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Chapter 62 : Commercial Production of Extracellular Enzymes

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Abstract:

This chapter discusses production strains and the regulation of extracellular-enzyme expression. The chapter also analyzes the properties of amylases and cellulases produced by spp., with comparisons to similar enzymes made by other microorganisms. Almost all of the extracellular enzymes in spp. are under temporal control (possibly because of their scavenging nature). Starch-degrading enzymes included such as cellulases, proteases and glucose isomerase are discussed in the chapter. Starch-degrading enzymes have different action patterns on starch and have been characterized by a number of different criteria. Cellulolytic enzymes include cellulases, cellulases and alkalophilic cellulases are discussed in the chapter. Cellulases of other gram-positive bacteria are also discussed. Through biochemical analyses of the microbial cellulases and comparisons of gene sequence homologies, predicted amino acid sequence homologies, and predicted structural similarities, several investigators have identified common functional domains and classified the cellulases into nine families. Current studies of the molecular genetics of will generate a better knowledge of the regulation of gene expression and of the mechanisms involved in translation and secretion. This knowledge will allow use of to express and secrete high volumes of homologous modified enzymes and heterologous gene products.

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62

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Figures

Image of Figure 1
Figure 1

Locations of binding sites of regulators on the subtilisin promoter. The regions protected from DNAse digestion by Hpr and Sin are boxed; the dashed line indicates the area of protection due to AbrB. This figure is courtesy of J. A. Hoch.

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62
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Image of Figure 2
Figure 2

Schematic representation of an amylopectin-type molecule, with an (1→6) branch point shown in more detail below. Potential cleavage sites for -amylases (A), -amylases (B), debranching enzymes (D; pullulanases or isoamylases), and glucoamylases (G) are indicated by arrows. The reducing end is indicated by a filled symbol.

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62
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Image of Figure 3
Figure 3

Seven regions of homology in amino acid sequence alignment of nine endoamylases chosen from different cluster groups ( Fig. 4 ). Computer alignments (Genetics Computer Group, Inc.) of the 34 amino acid sequences shown in Fig. 4 were determined by pairwise alignments of the most related sequences or sequence clusters ( ). Amino acids conserved in at least five of the nine sequences shown (O) and those conserved in all 34 sequences shown in Fig. 4 (♦) are indicated. Dashed lines indicate gaps in the sequences of various lengths, and a period represents a gap of one amino acid. Sequences are named by whether they were classified as an -amylase (A:), an -amylase-pullulanase (AP:), a CGTase (C:), or a pullulanase (P:) and by the organism from which they were isolated: (Bst), (Bme), (Cth), S. (Shy), (Bsu), sp. strain 17-1 (B17-1), (Bpo), or a gram-positive bacterium (G+). As in the text, numbering is given for the mature -amylase from and regions with putative catalytic and/or binding residues are denoted by uppercase roman numerals.

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62
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Image of Figure 4
Figure 4

Dendrogram illustrating the relationships among 34 endoamylases aligned as described in the legend to Fig. 3 . The nomenclature used is the same as in Fig. 3 . Additional classifications are isoamylase (I:), oligo-l,6-glucosidase (G:), dextran glucosidase (D:), neopullulanase (N:), maltogenic -amylase (Am:), and exoamylase (X:)· The sequences in order from top to bottom are: pullulanase (P:Kae; 77), pullulanase (P:Bst; 89), isoamylase (I:Pam; 1), oligo-1,6-glucosidase (G:Bce; 189), oligo-1,6-glucosidase (G:Bth; 188), S. dextran glucosidase (D:Smu; 139), -amylase (A:Bme; 102), -amylase-pullulanase (AP:Cth; 101), neopullulanase (N:Bst; 88), amylase (A:Dth; 63), -amylase (A:Bli; 198), -amylase (A:Bam; 166), sp. strain 707 -amylase (A:B707; 174), -amylase (A:Bst; 67), -amylase (A:Bsu; 195), -amylase (A:Bfi; 138), -amylase (A:Sli; 93), S. -amylase (A:Shy; 64), -amylase (A:Aha; 27), -amylase (A:Ahy; 47), sp. strain 1011 CGTase (C:B1011; 80), sp. strain 38-2 CGTase (C:B38-2; 75), sp. strain B1018 -amylase (A:B1018; 68), sp. strain 17-1 CGTase (C:B17-1; 76), -amylase (A:Bci; 115), -amylase (A:Cts; 3), CGTase (C:Bma; 163), CGTase (C:Boh; 147), maltogenic -amylase (Am:Bst; 22), CGTase (C:Kpn; 8), -amylase (A: Bpo; 175), -amylase (A:Aor; 190), exoamylase (X:Pst; 37), and gram-positive bacterium -amylase (A:G+; 13). Sequences from organisms that are not gram-positive bacteria were included for comparisons. For simplicity, some available sequences of endoamylases were not included, since most are similar to ones already used in the alignments ( ). The distance to the branch point connecting two sequences is proportional to the identity between the two sequences, as shown by the scale on this figure (for example, the amino acid sequences of A:Sli and A:Shy are 56% identical). In general, the inclusion of a sequence in a given group should be considered approximate when the sequence is less than 20% identical to the other members of the cluster group.

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62
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Figure 5

Comparison of protein sequences of cellulases from four different strains of Positions marked in boldface indicate differences between the strains. Designations are as follows: Bsu PAP115, PAP115 ( ); Bsu BSE616, BSE616 ( ); Bsu DLG, DLG ( ); BsulFO3034, IFO3034 ( ).

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62
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Image of Figure 6
Figure 6

Comparison of protein sequences of alkaline cellulases from bacilli. Consensus denotes a consensus sequence determined by position similarities in two or more sequences; uppercase amino acid symbols indicate similar or identical residues that generated the consensus sequence. Lowercase symbols designate differences from consensus sequence. Sequence designations are as follows: Bac N-4 CelA, strain N-4 endoglucanase A ( ); Bac N-4 CelB, ( ); Bac KSM-635, strain KSM-635 ( ); Bac str.1139, strain 1139 ( ); Bac N-4 CelC, strain N-4 endoglucanase C ( ).

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62
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References

/content/book/10.1128/9781555818388.chap62
1. Amemura, A.,, R. Chakraborty,, M. Fujita,, T. Noumi,, and M. Futai. 1988. Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amylodermamosa SB-15. J. Biol. Chem. 263:92719275.
2. Baecker, P. A., E. Greenburg, and J. Preiss. 1986. Biosynthesis of bacterial glycogen: primary structure of Escherichia coli l,4-α-D-glucan:l,4-α-D-glucan 6-α-D-(l,4-α-D-glucano)-transferase as deduced from the nucleotide sequence of the g/gB gene. J. Biol. Chem. 261: 87388743.
3. Bahl, H.,, G. Burchhardt,, A. Spreinat,, K. Haeckel,, A. Wienecke,, B. Schmidt,, and G. Antranikian. 1991. α-Amylase of Clostridium thermosulfurogenes EMI: nucleotide sequence of the gene, processing of the enzyme, and comparison to other α-amylases. Appl. Environ. Microbiol. 57:15541559.
4. Bahri, S. M.,, and J. M. Ward. 1990. Nucleotide sequence of an α-amylase gene isolated from Streptomyces thermolliolaceus CUB74. GenBank Genetic Sequence Data Bank, Release 68.0, Locus:Stmamy, Accession: M34957. Unpublished sequence.
5. Baird, S. K.,, D. A. Johnson,, and V. L. Seligy. 1990. Molecular cloning, expression, and characterization of endo-β-l,4-glucanase genes from Bacillus polymyxa and Bacillus circulans. J. Bacteriol. 172:15761586.
6. Bealin-Kelly, F.,, C. T. Kelly,, and W. M. Fogarty. 1991. Studies on the thermostability of the α-amylase of Bacillus caldovelox. Appl. Microbiol. Biotechnol. 36:332336.
7. Beguin, P. 1990. Molecular biology of cellulose degradation. Annu. Rev. Microbiol. 44:219248.
8. Binder, F.,, O. Huber,, and A. Bock. 1986. Cyclodextringlycosyltransferase from Klebsiella pneumoniae M5al: cloning, nucleotide sequence and expression. Gene 47: 269277.
9. Boel, E.,, L. Brady,, A. M. Brzozowski,, Z. Derewenda,, G. G. Dodson,, V. J. Jensen,, S. B. Petersen,, H. Swift,, L. Thim,, and H. F. Woldike. 1990. Calcium binding in α-amylases: an X-ray diffraction study at 2.1-Å resolution of two enzymes from Aspergillus. Biochemistry 29:62446249.
10. Boyer, E. W.,, and M. B. Ingle. 1972. Extracellular alkaline amylase from a Bacillus species. J. Bacteriol. 110:9921000.
11. Brosnan, M. P.,, C. T. Kelly,, and W. M. Fogarty. 1992. Investigation of the mechanisms of irreversible thermoinactivation of Bacillus stearothermophilus α-amylase. Eur. J. Biochem. 203:225231.
12. Buisson, G.,, E. Duee,, R. Haser,, and F. Payan. 1987. Three dimensional structure of porcine pancreatic α-amylase at 2.9-Å resolution. Role of calcium in structure and activity. EMBO J. 6:39093916.
13. Candussio, A.,, G. Schmid,, and A. Bock. 1990. Biochemical and genetic analysis of a maltopentaose-producing amylase from an alkaliphilic Gram-positive bacterium. Eur. J. Biochem. 191:177185.
14. Cheetam, P. S. J. 1985. The applications of enzymes to industry, p. 274379. In A. Wiseman (ed.), Handbook of Enzyme Biotechnology, 2nd ed. Ellis Horwood Ltd., Chichester, United Kingdom.
15. Chojecki, A.,, and H. P. Blaschek. 1986. Effect of carbohydrate source on alpha-amylase and glucoamylase formation by Clostridium acetobutylicum SA-1. J. Ind. Microbiol. 1:6367.
16. Chu, K. (Genencor International). 1992. Personal communication.
17. Coughlan, M. P., 1990. Cellulose degradation by fungi, p. 136. In W. M. Fogarty, and C. T. Kelly (ed.), Microbial Enzymes and Biotechnology, 2nd ed. Elsevier Applied Science, New York.
18. Dahl, M. K.,, T. Msadek,, F. Kunst,, and G. Rapoport. 1991. Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase. J. Bacteriol. 173:25392547.
19. Debabov, V. G., 1982. The industrial use of bacilli, p. 331370. In D. A. Dubnau (ed.). The Molecular Biology of the Bacilli. Academic Press, Inc., New York.
20. Declerck, N.,, P. Joyet,, C. Gaillardin,, and J.-M. Masson. 1990. Use of amber suppressors to investigate the thermostability of Bacillus licheniformis α-amylase. J. Biol. Chem. 265:1548115488.
21. Demain, A. L., 1990. Regulation and exploitation of enzyme biosynthesis, p. 331368. In W. M. Fogarty, and K. T. Kelly (ed.), Microbial Enzymes and Biotechnology, 2nd ed. Elsevier Applied Science, London.
22. Dlderichsen, B.,, and L. Christiansen. 1988. Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus. FEMS Microbiol. Lett. 56:5360.
23. Dod, B.,, and G. Balassa. 1978. Spore control (sco) mutations in Bacillus subtilis. III. Regulation of extracellular protease synthesis in the spore control mutations scoC. Mol. Gen. Genet. 163:5763.
24. Doi, R. H. 1991. Proteolytic activities in Bacillus. Curr. Opin. Biotechnol. 2:682684.
25. Dordlck, J. S. 1991. An introduction to industrial bio-catalysis, p. 319. In J. S. Dordick (ed.), Biocatalysts for Industry. Plenum Press, New York.
26. Emori, M.,, and B. Maruo. 1988. Complete nucleotide sequence of an α-amylase from Bacillus subtilis 2633, an amylase extrahyperproducing strain. Nucleic Acids Res. 16:7178,
27. Feller, G.,, T. Lonhienne,, C. Deroanne,, C. Libioulle,, J. Von Beeumen,, and C. Gerday. 1992. Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychotroph Alteromonas haloplanctis A23. J. Biol. Chem. 267:52175221.
28. Feng, D.-F.,, and R. F. Doolittle. 1987. Progressive sequence alignments as a prerequisite to correct phylogenetic trees. J. Mol. Evol. 35:351360.
29. Ferrari, E.,, D. J. Henner,, M. Perego,, and J. A. Hoch. 1988. Transcription of Bacillus subtilis subtilisin and expression of subtilisin in sporulation mutation. J. Bacteriol. 170:289295.
30. Ferrari, E.,, S. M>,. H. Howard,, and J. A. Hoch. 1986. Effect of stage 0 sporulation mutations on subtilisin expression. J. Bacteriol. 166:173179.
31. Ferrari, E.,, and M. Ruppen. Unpublished data.
32. Fogarty, W. M.,, and E. J. Bourke. 1983. Production and purification of a maltose-producing amylase from Bacillus subtilis IMD 198. J. Chem. Technol. Biotechnol. 33B:145151.
33. Folkman, J.,, P. B. Weisz,, M. M. Joullié, W. W. Li,, and W. R. Ewing. 1989. Control of angiogenesis with synthetic heparin substitutes. Science 243:14901493.
34. French, D., 1975. Chemistry and biochemistry of starch, vol. 5, p. 267335. In W. J. Whelan (ed.), MTP International Review of Science. University Park Press, Baltimore.
35. Friedberg, F.,, and C. Rhodes. 1986. Cloning and characterization of the beta-amylase gene from Bacillus polymyxa. J. Bacteriol. 165:819824.
36. Friedman, R. B., 1991. Linear and cyclic dextrins, p. 327347. In I. Goldberg, and R. Williams (ed.), Biotechnology and Food Ingredients. Van Nostrand Reinhold, New York.
37. Fujita, M.,, K. Torigoe,, T. Nakada,, K. Tsusaki,, M. Kubota,, S. Sakai,, and Y. Tsujisaka. 1989. Cloning and nucleotide sequence of the gene (amyP) for maltotet-raose-forming amylase from Pseudomonas stutzeri MO-19. J. Bacteriol. 171:13331339.
38. Fukumori, F.,, T. Kudo,, and K. Horikoshi. 1985. Purification and properties of a cellulase from alkalophilic Bacillus sp. no. 1139. J. Gen. Microbiol. 131:33393345.
39. Fukumori, F.,, T. Kudo,, and K. Horikoshi. 1987. Truncation analysis of an alkaline cellulase from an alkalophilic Bacillus species. FEMS Microbiol. Lett. 40:311314.
40. Fukumori, F.,, T. Kudo,, Y. Narahashi,, and K. Horikoshi. 1986. Molecular cloning and nucleotide sequence of the alkaline cellulase gene from the alkalophilic Bacillus sp. strain 1139.J. Gen. Microbiol. 132:23292335.
41. Fukumori, F.,, T. Kudo,, N. Sashihara,, Y. Nagata,, K. Ito,, and K. Horikoshi. 1989. The third cellulase of alkalophilic Bacillus sp. strain N-4: evolutionary relationships within the cel gene family. Gene 76:289298.
42. Fukumori, F.,, K. Ohishi,, T. Kudo,, and K. Horikoshi. 1987. Tandem location of the cellulase genes on the chromosome of Bacillus sp. strain N-4. FEMS Microbiol. Lett. 48:6568.
43. Fukumori, F.,, N. Sashihara,, T. Kudo,, and K. Horikoshi. 1986. Nucleotide sequences of two cellulase genes from alkalophilic Bacillus sp. strain N-4 and their strong homology. J. Bacteriol. 168:479485.
44. Gaur, G. K.,, J. Oppenheim,, and I. Smith. 1991. The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein. J. Bacteriol. 173:678686.
45. Gilkes, N. R.,, B. Henrissat,, D. G. Kilburn,, R. C. Miller,, Jr., and R. A. J. Warren. 1991. Domains in microbial β-1,4-gIycanases: sequence conservation, function, and enzyme families. Microbiol. Rev. 55:303315.
46. Gilkes, N. R.,, R. A. J. Warren,, R. C. Miller,, Jr., and D. G. Kilburn. 1988. Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J. Biol. Chem. 263:1040110407.
47. Gobius, K. S.,, and J. M. Pemberton. 1988. Molecular cloning, characterization, and nucleotide sequence of an extracellular amylase gene from Aeromonas hydrophila.J. Bacteriol. 170:13251332.
48. Godtfredsen, S. E., 1990. Microbial lipases, p. 255274. In W. M. Fogarty, and K. T. Kelly (ed.), Microbial Enzymes and Biotechnology, 2nd ed. Elsevier Applied Science, London.
49. Gray, G. L.,, S. E. Mainzer,, M. W. Rey,, M. H. Lamsa,, K. L. Kindle,, C. Carmona,, and C. Requadt. 1986. Structural genes encoding the thermophilic α-amylases of Bacillus stearothermophilus and Bacillus licheniformis. J. Bacteriol. 166:635643.
50. Graycar, T. P., 1991. Protein engineering of subtilisin, p. 257284. In J. S. Dordick (ed.), Biocatalysts for Industry. Plenum Press, New York.
51. Hacking, J. A., 1991. Biocatalysis in the production of carbohydrates for food uses, p. 6382. In J. S. Dordick (ed.), Biocatalysts for Industry. Plenum Press, New York.
52. Henner, D. J.,, E. Ferrari,, M. Perego,, and J. A. Hoch. 1988. Location of the target of the hpr-97, sacU32(Hy), and sacQ36(Hy) mutations in upstream region of the subtilisin promoter. J. Bacteriol. 170:296300.
53. Henner, D. J.,, M. Yang,, L. Band,, H. Shimotsu,, M. Ruppen,, and E. Ferrari,. 1986. Genes of Bacillus subtilis which regulate the expression of degradative enzymes, p. 8190. In M. Alacevic,, D. Hranueli,, and Z. Toman (ed.), Genetics of Industrial Microorganisms. Proceedings of the Fifth International Symposium on the Genetics of Industrial Microorganisms. Ognjen Prica Printing Works, Karlovac, Yugoslavia.
54. Henner, D. J.,, M. Yang,, and E. Ferrari. 1988. Localization of the Bacillus subtilis sacU(Hy) mutations to two linked genes with similarities to the conserved procaryotic family of two-component signalling systems. J. Bacteriol. 170:51025109.
55. Henrissat, B.,, M. Claeyssens,, P. Tonune,, L. Lemesle,, and J.-P. Mornon. 1989. Cellulase families revealed by hydrophobic cluster analysis. Gene 81:8395.
56. Higashihara, M.,, and H. Okada. 1974. Studies on beta-amylase of Bacillus megaterium no. 31. Agric. Biol. Chem. 38:10231029.
57. Hill, D. E.,, R. Aldape,, and J. D. Rozzell. 1990. Nucleotide sequence of a cyclodextrin glucosyltransferase gene, cgtA, from Bacillus licheniformis. Nucleic Acids Res. 18:199.
58. Hitosuyanagi, K.,, K. Yamane,, and B. Maruo. 1979. Stepwise introduction of regulatory genes stimulating production of α-amylase into Bacillus subtilis: construction of an α-amylase extrahyperproducing strain. Agric. Biol. Chem. 43:23432349.
59. Hoch, J. A. 1976. Genetics of bacterial sporulation. Adv. Genet. 18:6998.
60. Holm, L.,, A. K. Koivula,, P. M. Lehtovaara,, A. Hemminki,, and J. K. C. Knowles. 1990. Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus alpha-amylase. Protein Eng. 3:181191.
61. Honjo, M.,, A. Nakayama,, K. Fukazawa,, K. Kawamura,, K. Ando,, M. Hori,, and Y. Furutanl. 1990. A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production. J. Bacteriol. 172:17831790.
62. Horikoshi, K.,, M. Nakao,, Y. Kurono,, and N. Sashlhara. 1984. Cellulases of an alkalophilic Bacillus strain isolated from soil. Can. J. Microbiol. 30:774779.
63. Horinouchi, S.,, S. Fukusumi,, T. Ohshima,, and T. Beppu. 1988. Cloning and expression in Escherichia coli of two additional amylase genes of a strictly anaerobic thermophile, Dictyoglomus thermophilum, and their nucleotide sequences with extremely low guanine-plus-cytosine contents. Eur J. Biochem. 176:243253.
64. Hoshiko, S.,, O. Makabe,, C. Nojiri,, K. Katsumata,, E. Satoh,, and K. Nagaoka. 1987. Molecular cloning and characterization of the Streptomyces hygroscopicus α-amylase gene. J. Bacteriol. 169:10291036.
65. Howard, G. T.,, and B. A. White. 1988. Molecular cloning and expression of cellulase genes from Rumonococcus albus 8 in Escherichia coli bacteriophage A. Appl. Environ. Microbiol. 54:17521755.
66. Hyun, H. H.,, and J. G. Zelkus. 1985. General biochemical characterization of thermostable pullulanase and glucoamylase from Clostridium thermohydrosulfuricum. Appl. Environ. Microbiol. 49:11681173.
67. Ihara, H.,, T. Sasaki,, A. Tsuboi,, H. Yamagata,, N. Tsukagoshi,, and S. Udaka. 1985. Complete nucleotide sequence of a thermophilic α-amylase gene: homology between prokaryotic and eukaryotic α-amylases at the active sites. J. Biochem. 98:95103.
68. Itkor, P.,, N. Tsukagoshi,, and S. Udaka. 1990. Nucleotide sequence of the raw-starch-digesting amylase gene from Bacillus sp. B1018 and its strong homology to the cyclodextrin glucanotransferase genes. Biochem. Biophys. Res. Commun. 166:630636.
69. Ito, S.,, S. Shikata,, K. Ozaki,, S. Kawai,, K. Okamoto,, S. Inoue,, A. Takei,, Y. Ohta,, and T. Satoh. 1989. Alkaline cellulase for laundry detergents: production by Bacillus sp. KSM-635 and enzymatic properties. Agric. Biol. Chem. 53:12751281.
70. Jarnagln, A. S.,, and E. Ferrari. 1992. Extracellular enzymes: gene regulation and structure function relationship studies, p. 191219. In R. Doi and M. McGloughlin (ed.), Biology of Bacilli: Applications to Industry. Butterworth-Heinemann, Boston.
71. Jergensen, P. L.,, and C. K. Hansen. 1990. Multiple endo-β-l,4-glucanase-encoding genes from Bacillus lautus PL236 and characterization of the celB gene. Gene 93:5560.
72. Jergensen, P. L.,, G. B. Poulsen,, and B. Diderichsen. 1991. Cloning of a chromosomal α-amylase gene from Bacillus stearothermophilus. FEMS Microbiol. Lett. 77: 271276.
73. Kainuma, K., 1984. Starch oligosaccharides: linear, branched, and cyclic, p. 125|–152. In R. L. Whistler,, J. N. Bemiller, and E. F. Paschall (ed.), Starch: Chemistry and Technology, 2nd ed. Academic Press, Inc., Orlando, Fla.
74. Kallio, P. T.,, J. E. Fagelson,, J. A. Hoch,, and M. A. Strauch. 1991. The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein. J. Biol. Chem. 266:1341113417.
75. Kaneko, P.,, T. Hamamoto,, and K. Horikoshi. 1988. Molecular cloning and nucleotide sequence of the cyclomaltodextrin glucanotransferase gene from the alkalophilic Bacillus sp. strain no. 38-2. J. Gen. Microbiol. 134:97105.
76.Kaneko, T., K. Song, T. Hamamoto, T. Kudo, and K. Horikoshi. 1989. Construction of a chimeric series of Bacillus cyclomaltodextrin glucanotransferases and analysis of the thermal stabilities and pH optima of the enzymes. J. Gen. Microbiol. 135:34473457.
77.Katsuragi, N., N. Takizawa, and Y. Murooka. 1987. Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. J. Bacteriol. 169:23012306.
78. Kawai, S.,, K. Oshino,, H. Okoshi,, H. Mori,, K. Ara,, S. Ito,, and K. Okamoto. 1988. Alkali resistant cellulases and microorganisms capable of producing same. European patent application EP 270974 A2.
79.Kawazu, T., Y. Nakanishl, N. Uozumi, T. Sasaki, H. Yamagata, N. Tsukagoshi, and S. Udaka. 1987. Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa β-amylase. J. Bacteriol. 169:15641570.
80. Kimura, K.,, S. Kataoka,, Y. Ishil,, T. Takano,, and K. Yamane. 1987. Nucleotide sequence of the β-cyclo-dextrin glucanotransferase gene of alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid sequence to those of α-amylases. J. Bacteriol. 169:43994402.
81. Kindle, K. L. 1983. Characteristics and production of thermostable α-amylase. Biochem. Biotechnol. 8:153170.
82.Kitamoto, N., H. Yamagata, T. Kato, N. Tsukagoshi, and S. Udaka. 1988. Cloning and sequencing of the gene encoding thermophilic β-amylase of Clostridium thermosulfurogenes. J. Bacteriol. 170:58485854.
83.Klein, C, and G. E. Schulz. 1991. Structure of cyclodextrin glycosyltransferase refined at 2.0Å resolution. J. Mol. Biol. 217:737750.
84. Koide, Y.,, A. Nakamura,, T. Uozumi,, and T. Beppu. 1986Wrong number of periods to parse title/source. Molecular cloning of a cellulase gene from Bacillus subtilis and its expression in Escherichia coli. Agric. Biol. Chem. 56:233237.
85.Kondo, H., H. Nakatani, R. Matsuno, and K. Hiromi. 1980. Product distribution in amylase catalyzed hydrolysis of amylose: comparison of experimental results with theoretical predictions. J. Biochem. 87:10531070.
86.Krels, M., M. Williamson, B. Buxton, J. Pywell, J. Hejgaard, and I. Svendsen. 1987. Primary structure and differential expression of β-amylase in normal and mutant barleys. Eur. I. Biochem. 169:517525.
87. Kunst, F.,, M. DebarbouiUle,, T. Msadek,, M. Young,, C. Mauel,, D. Karamata,, A. Klier,, G. Rapoport,, and R. Dedonder. 1988. Deduced polypeptides encoded by the Bacillus subtilis sacU locus share homology with two-component sensor regulatory systems. J. Bacteriol. 170: 50935101.
88. Kuriki, T.,, and T. Imanaka. 1989. Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. J. Gen. Microbiol. 135:15211528.
89. Kuriki, T.,, J.-H. Park,, and T. Imanaka. 1990. Characteristics of thermostable pullulanase from Bacillus stearothermophilus and the nucleotide sequence of the gene. J. Ferment. Bioeng. 69:204210.
90. Lao, G.,, G. S. Ghangas,, E. D. Jung,, and D. B. Wilson. 1991. DNA sequences of three β-1,4-endoglucanase genes from Thermomonospora fusca. J. Bacteriol. 173: 33973407.
91. Lepesant, J. A., F. Kunst, J. Lepesant-Kejzlarova, and R. Dedonder. 1972. Chromosomal location of the mutations affecting sucrose metabolism in Bacillus subtilis Marburg. Mol. Gen. Genet. 118:135160.
92. Lo, A. C, R. M. MacKay, V. L. Seligy, and G. E. Wlllick. 1988. Bacillus subtilis β-1,4-endoglucanase products from intact and truncated genes are secreted into the extracellular medium by Escherichia coli. Appl. Environ. Microbiol. 54:22872292.
93. Long, C. M.,, M.-J. Vlrolle,, S.-Y. Chang,, S. Chang,, and M. J. Bibb. 1987. α-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate α-amylases. J. Bacteriol. 169:57455754.
94.MacGregor, E. A., and B. Svensson. 1989. A super-secondary structure predicted to be common to several a-l,4-D-glucan-cleaving enzymes. Biochem. J. 259:145152.
95. MacKay, R. M.,, S. Baird,, M. J. Dove,, J. A. Erratt,, M. Glnes,, F. Moranelli,, A. Nasim,, G. E. Wlllick,, M. Yaguchi,, and V. L. Seligy. 1985. Glucanase gene diversity in prokaryotic and eukaryotic organisms. BioSystems 18: 279292.
96. MacKay, R. M.,, A. Lo,, G. WiUick,, M. Zuker,, S. Baird,, M. Dove,, F. Moranelli,, and V. Seligy. 1986. Structure of a Bacillus subtilis endo-β-l,4-glucanase gene. Nucleic Acids Res. 14:91599170.
97. MacQultty, J. J. 1988. Impact of biotechnology on the chemical industry, p. 11-29. In M. P. Phillips, S. P. Shoemaker, R. D. Middlekauff, and R. M. Ottenbrite (ed.), The Impact of Chemistry on Biotechnology: Multi-disciplinary Discussion. American Chemical Society, Washington, D.C.
98. Marshall, J. J. 1974. Characterization of Bacillus polymyxa amylase as an exo-acting(l-4)alpha-D-glucan maltohydrolase. FEBS Lett. 46:14.
99.Matsuura, Y., M. Kusunoki, W. Harada, and M. Kakudo. 1984. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. 95:697702.
100.Meinke, A., N. R. Gilkes, D. G. Kilburn, R. C. Miller, Jr., and R. A. J. Warren. 1991. Multiple domains in endoglucanase B (cenB) from Cellulomonas fimi: functions and relatedness to domains in other polypeptides. J. Bacteriol. 173:71267135.
101.Melasniemi, H., M. Palohelmo, and L. Hemid. 1990. Nucleotide sequence of the α-amylase-pullulanase gene from Clostridium thermohydrosulfuricum. J. Gen. Microbiol. 136:447454.
102. Metz, R. J.,, L. N. Allen, T. M. Cao, and N. W. Zeman. 1988. Nucleotide sequence of an amylase gene from Bacillus megaterium. Nucleic Acids Res. 16:5203.
103.Mikami, B., Y. Morita, and C. Fukazawa. 1988. Primary structure and function of β-amylase. Seikagaku 60:211216.
104.Msadek, T., M. K. Dahl, F. Kunst, and G. Rapoport. 1992. The DegS/DegU signal transduction pathway in Bacillus subtilis, abstr. 17. Program Abstr. 11th Int. Spore Conf.
105. Msadek, T.,, F. Kunst,, D. J. Henner,, A. Klier,, G. Rapoport,, and R. Dedonder. 1990. Signal transduction pathway controlling synthesis of class of degradative enzymes in Bacillus subtilis: expression of the regulatory genes and analysis of mutations in degS and degU. J. Bacteriol. 172:824834.
106. Mukai, K.,, M. Kawata,, and T. Tanaka. 1990. Isolation and phosphorylation of the Bacillus subtilis degS and degU gene products. J. Biol. Chem. 265:2000020006.
107. Nagashlma, T.,, S. Tada,, K. Kitamoto,, K. Gomi,, C. Kumagai,, and H. Toda. 1992. Site-directed mutagenesis of catalytic active-site residues of Taka-amylase A. Biosci. Biotechnol. Biochem. 56:207210.
108. Nakai, R.,, S. Horinouchi,, and T. Beppu. 1988. Cloning and nucleotide sequence of a cellulase gene, casA, from an alkalophilic Streptomyces strain. Gene 65:229238.
109. Nakai, R.,, S. Horinouchi,, T. Uozumi,, and T. Beppu. 1987. Purification and properties of cellulases from an alkalophilic Streptomyces strain. Agric. Biol. Chem. 51: 30613065.
110. Nakajima, R.,, T. Imanaka,, and S. Alba. 1985. Nucleotide sequence of the Bacillus stearothermophilus α-amylase gene. J. Bacteriol. 163:401406.
111. Nakajima, R.,, T. Imanaka,, and S. Alba. 1986. Comparison of amino acid sequences of eleven different α-amylases. Appl. Microbiol. Biotechnol. 23:355360.
112.Nakamura, A., F. Fukumori, S. Horinouchi, H. Masaki, T. Kudo, T. Uozumi, K. Horikoshi, andT. Beppu. 1991. Construction and characterization of the chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase. J. Biol. Chem. 266:15791583.
113.Nakamura, A., K. Haga, S. Ogawa, K. Kuwano, K. Klmura, K. Yamane. 1992. Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α-amylases: site-directed mutagenesis of the conserved two Asp and one Glu residues. FEBS Lett. 296:3740.
114.Nakamura, A., T. Uozumi, and T. Beppu. 1987. Nucleotide sequence of a cellulase gene of Bacillus subtilis. Eur. J. Biochem. 164:317320.
115. Nlshizawa, M.,, F. Ozawa,, and F. Hishinuma. 1987. Molecular cloning of an amylase gene of Bacillus circulars. DNA 6:255265.
116. Nitschke, L.,, K. Heeger,, H. Bender,, and G. E. Schulz. 1990. Molecular cloning, nucleotide sequence and expression in Escherichia coli of the β-cyclodextrin glyco-syltransferase gene from Bacillus circulans strain no. 8. Appl. Microbiol. Biotechnol. 33:542546.
117.Ohmlya, K., T. Kajino, A. Kato, and S. Shimizu. 1989. Structure of a Ruminococcus albus endo-l,4-β-gluca-nase gene. J. Bacteriol. 171:67716775.
118. O'Neill, G. P.,, S. H. Goh,, R. A. J. Warren,, D. G. Kilburn,, and R. C. Miller, Jr. 1986. Structure of the gene encoding the exoglucanase of Cellulomonas fimi. Gene 44:325330.
119. Outtrup, H., and B. E. Norman. 1984. Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques. Starch Starke 36:405411.
120. Ozaki, K.,, and S. Ito. 1991. Purification and properties of an acid endo-l,4-0-glucanase from Bacillus sp. KSM-330.1. Gen. Microbiol. 137:4148.
121. Ozaki, K.,, S. Shikata,, S. Kawai,, S. Ito,, and K. Okamoto. 1990. Molecular cloning and nucleotide sequence of a gene for alkaline cellulase from Bacillus sp. KSM-635. J. Gen. Microbiol. 136:13271334.
122. Park, S. H., H. K. Kim, and M. Y. Pack. 1991. Characterization and structure of the cellulase gene of Bacillus subtilis BSE616. Agric. Biol. Chem. 55:441448.
123. Park, S. H., and M. Y. Pack. 1986. Cloning and expression of a Bacillus cellulase gene in Escherichia coli. Enzyme Microb. Technol. 8:725728.
124. Perego, M.,, and J. A. Hoch. 1988. Sequence analysis and regulation of the hpr locus, a regulatory gene for protease production and sporulation in Bacillus subtilis. J. Bacteriol. 170:25602567.
125. Perego, M.,, G. B. Spiegelman,, and J. A. Hoch. 1988. Structure of the gene for the transition state regulator AbrB: regulator synthesis is controlled by the Spo0A protein. Mol. Microbiol. 2:689699.
126. Petficek, M.,, P. Tichy,, and M. Kuncova. 1992. Characterization of the α-amylase-encoding gene from Ther momonospora curvata. Gene 112:7783.
127. Poole, D. M.,, G. P. Hazlewood,, J. I. Laurie,, P. J. Barker,, and H. J. Gilbert. 1990. Nucleotide sequence of the Ruminococcus albus SY3 endoglucanase genes celA and celB. Mol. Gen. Genet. 223:217223.
128. Priest, F. G. 1977. Extracellular enzyme synthesis in the genus Bacillus. Bacteriol. Rev. 41:711753.
129. Priest, F. G. 1984. Extracellular enzymes, p. 5462. American Society for Microbiology, Washington, D.C.
130. Priest, F. G.,, M. Goodfellow,, and C. Todd. 1988. A numerical classification of the genus Bacillus. J. Gen. Microbiol. 134:18471882.
131. Reilly, P. J., 1985. Enzymic degradation of starch, p. 101142. In G. M. A. van Beynum, and J. A. Roels (ed.), Starch Conversion Technology. Marcel Dekker, Inc., New York.
132.Rhodes, C, J. Strasser, and F. Friedberg. 1987. Sequence of an active fragment of B. polymyxa beta amylase. Nucleic Acids Res. 15:3934.
133. Robson, L. M.,, and G. H. Chambliss. 1986. Cloning of the Bacillus subtilis DLGβ-l,4-glucanase gene and its expression in Escherichia coli and B. subtilis. J. Bacteriol. 165:612619.
134. Robson, L. M.,, and G. H. Chambliss. 1987. Endo-β-l,4-glucanase gene of Bacillus subtilis DLG. J. Bacteriol. 169:20172025.
135. Robson, L. M.,, and G. H. Chambliss. 1989. Cellulases of bacterial origin. Enzyme Microb. Technol. 11:626644.
136. Robyt, J. F., 1984. Enzymes in the hydrolysis and synthesis of starch, p. 87123. In R. L. Whistler,, J. N. Bemiller,, and E. F. Paschall (ed.), Starch: Chemistry and Technology, 2nd ed. Academic Press, Inc., Orlando, Fla.
137. Rogers, J. C. 1985. Conserved amino acid sequence domains in alpha-amylases from plants, mammals, and bacteria. Biochem. Biophys. Res. Commun. 128:470476.
138. Rumbak, E.,, D. E. Rawlings,, G. G. Lindsey,, and D. R. Woods. 1991. Cloning, nucleotide sequence, and enzymatic characterization of an α-amylase from the rumi-nal bacterium Butyrivibrio fibrisolvens H17c. J. Bacteriol. 173:42034211.
139. Russell, R. R. B.,, and J. J. Ferretti. 1990. Nucleotide sequence of the dextran glucosidase (dexB) gene of Streptococcus mutans. J. Gen. Microbiol. 136:803810.
140. Saha, B. C, and J. G. Zeikus. 1989. Novel highly thermostable pullulanase from thermophiles. Trends Biotechnol. 7:234239.
141.Sashihara, N., T. Kudo, and K. Horikoshi. 1984. Molecular cloning and expression of cellulase genes to alkalophilic Bacillus sp. strain N-4 in Escherichia coli. J. Bacteriol. 158:503506.
142. Schmid, G.,, A. Englbrecht,, and D. Schmid,. 1988. Cloning and nucleotide sequence of a cyclodextrin glycosyl-transferase gene from the alkalophilic Bacillus 1-1, p. 7176. In O. Huber, and J. Szejdi (ed.). Proceedings of the Fourth International Symposium on Cyclodextrins. Kluwer Academic Publishers, New York.
143. Shen, G.-J.,, K. C. Srivastava,, Y. Wang,, and H. Y. Wang. March 1992. U.S. patent 5,093,256.
144. Shinke, R.,, H. Nishira,, and M. Mugibayashi. 1974. Isolation of β-amylase producing microorganisms. Agric. Biol. Chem. 38:665666.
145. Siggens, K. W. 1987. Molecular cloning and characterization of the beta-amylase gene from Bacillus circulans. Mol. Microbiol. 1:8691.
146. Siggens, K. W. 1987. Bacillus circulans gene for β-amylase. GenBank Genetic Sequence Data Bank, Release 68.0, Locus:Bacamyb, Accession: Y00523. Unpublished sequence.
147. Sin, K.,, A. Nakamura,, K. Kobayashi,, H. Masaki,, and T. Uozumi. 1991. Cloning and sequencing of a cyclodextrin glucanotransferase gene from Bacillus ohbensis and its expression in Escherichia coli. Appl. Microbiol. Biotechnol. 35:600605.
148. Slominska, L.,, and M. Maczynski. 1985. Studies on the application of pullulanase in starch saccharification process. Starch Starke 37:386390.
149. Smith, I., 1989. Initiation of sporulation, p. 185209. In I. Smith,, R. Slepecky,, and P. Setlow (ed.), Regulation of Procaryotic Development. American Society for Microbiology, Washington, D.C.
150. Specka, U.,, F. Mayer,, and G. Antranikian. 1991. Purification and properties of a thermoactive glucoamylase from Clostridium thermosaccharolyticum. Appl. Environ. Microbiol. 57:23172323.
151. Srivastava, R. A. K. 1984. Studies on extracellular and intracellular purified amylases from a thermophilic Bacillus stearothermophilus. Enzyme Microb. Technol. 6:422426.
152.Strauch, M. A., and J. A. Hoch. 1992. Control of postex-ponential gene expression by transition state regulators, p. 105121. In R. H. Doi, and M. McGloughlin (ed.), Biology of Bacilli: Applications to Industry. Butterworth-Heinemann, Boston.
153.Strauch, M. A., M. Perego, D. Burbulys, and J. A. Hoch. 1989. The transition state regulator AbrB of Bacillus subtilis is autoregulated during vegetative growth. Mol. Microbiol. 3:12031209.
154.Strauch, M. A., G. B. Spiegelman, M. Perego, W. C. Johnson, D. Burbulys, and J. A. Hoch. 1989. The transition state transcription regulator abrB of Bacillus subtilis is a DNA binding protein. EMBO J. 8:16151621.
155. Strauch, M. A.,, V. Webb,, G. Spiegelman,, and J. A. Hoch. 1990. The Spo0A protein of Bacillus subtilis is a repressor of the abrB gene. Proc. Natl. Acad. Set. USA 87:18011805.
156. Stutzenberger, F., 1990. Bacterial cellulases, p. 3770. In W. M. Fogarty,, and K. T. Kelly (ed.), Microbial Enzymes and Biotechnology, 2nd ed. Elsevier Applied Science, London.
157. Suominen, I.,, M. Karp,, J. Lautano,, J. Knowles,, and P. Mantsala,. 1987. Thermostable α-amylase of Bacillus stearothermophilus: cloning, expression and secretion by Escherichia coli, p. 129137. In J. Chaloupka, and V. Krumphanzl (ed.), Extracellular Enzymes of Microorganisms. Plenum Press, New York.
158.Suzuki, Y., K. Hatagakl, and H. Oda. 1991. A hyper-thermostable pullulanase produced by an extreme ther-mophile. Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability. Appl. Microbiol. Biotechnol. 34:707714.
159. Suzuki, Y.,, N. Ito,, T. Yuuki,, H. Yamagata,, and S. Udaka. 1989. Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation. J. Biol. Chem. 264:1893318938.
160.Suzuki, Y., K. Oishi, H. Nakano, and T. Nagayama. 1987. A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-l,6-glucosidases. Appl. Microbiol. Biotechnol. 26:546551.
161. Svensson, B. 1988. Regional distant sequence homology between amylases, α-glucosidases and transglucanosylases. FEBS Lett. 230:7276.
162.Svensson, B., H. Jespersen, M. R. Sierks, and E. A. MacGregor. 1989. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem. J. 264:309311.
163.Takano, T., M. Fukuda, M. Monma, S. Kobayashi, K. Kainuma, and K. Yamane. 1986. Molecular cloning, DNA nucleotide sequencing, and expression in Bacillus subtilis cells of the Bacillus macerans cyclodextrin glucanotransferase gene. J. Bacteriol. 166:11181122.
164. Takasaki, Y. 1976. Production and utilization of β-amylase and pullulanase from Bacillus cereusAgric. Biol. Chem var. 40:15151522.
165.Takase, K., T. Matsumoto, H. Mizuno, and K. Yamane. 1992. Site-directed mutagenesis of active site residues in Bacillus subtilis α-mycoides. Agric. Biol. Chem. amylase. Biochim. Biophys. Acta 1120:281288.
166. Takkinen, K.,, R. F. Pettersson,, N. Kalkkinen,, I. Palva,, H. Soderiund,, and L. Kaarialnen. 1983. Amino acid sequence of α-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J. Biol. Chem. 258:10071013.
167.Taniguchi, H., M. J. Chung, N. Yoshigi, and Y. Maruyama. 1983. Purification of Bacillus circulans F-2 amylase and its general properties. Agric. Biol. Chem. 47: 511520.
168.Tao, B. Y., P. J. Reilly, and J. F. Robyt. 1989. Dectection of a covalent intermediate in the mechanism of action of porcine pancreatic α-amylase by using l3C nuclear magnetic resonance. Biochim. Biophys. Acta 995:214220.
169. Thomas, J. A., and J. D. Allen. 1976. Subsite mapping of enzymes, collecting and processing experimental data: a case study of an amylase malto oligosaccharide system. Carbohydr. Res. 48:105124.
170. Thomas, M.,, F. G. Priest,, and J. R. Stark. 1980. Characterization of an extracellular β-amylase from Bacillus megaterium sensu stricto. J. Gen. Microbiol. 118:6772.
171. Tomazic, S. J.,, and A. M. Klibanov. 1988. Mechanisms of irreversible thermal inactivation of Bacillus α-amylases. J. Biol. Chem. 263:30863091.
172. Tomazlc, S. J.,, and A. M. Klibanov. 1988. Why is one Bacillus α-amylase more resistant against irreversible thermoinactivation than another? J. Biol. Chem. 263: 30923096.
173. Tomme, P.,, H. Van TUbeurgh,, G. Pettersson,, J. Van Damme,, J. Vandekerckhove,, J. Knowles,, T. Teeri,, and M. Claeyssens. 1988. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Eur. J. Biochem. 170:575581.
174.Tsukamoto, A., K. Kimura, Y. Ishii, T. Takano, and K. Yamane. 1988. Nucleotide sequence of the maltohexaose producing amylase gene from an alkalophilic Bacillus sp. #707 and structural similarity to liquefying type α-amylases. Biochem. Biophys. Res. Commun. 151: 2531.
175.Uozumi, N., K. Sakurai, T. Sasaki, S. Takekawa, H. Yamagata, N. Tsukagoshi, and S. Udaka. 1989. A single gene directs synthesis of a precursor protein with β-and α-amylase activities in Bacillus polymyxa. J. Bacteriol. 171:375382.
176.Valle, F, and E. Ferrari. 1989. Subtilisin: a redundantly temporally regulated gene?, p. 131146. In I. Smith,, R. Slepecky,, and P. Setiow (ed.). Regulation of Procaryotic Development. American Society for Microbiology, Washington, D.C.
177. Van TUbeurgh, H.,, P. Tomme,, M. Claeyssens,, R. Bhikhabhai,, and G. Pettersson. 1986. Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei. Separation of functional domains. FEBS Lett. 204:223227.
178. Vigal, T.,, J. A. Gil,, A. Daza,, M. D. García-González,, and J. F. Martin. 1991. Cloning, characterization and expression of an α-amylase gene from Streptomyces griseus IMRU3570. Mol. Gen. Genet. 225:278288.
179. Vlhinen, M.,, and P. Mäntsälä. 1989. Microbial amylolytic enzymes. Crit. Rev. Biochem. Mol. Biol. 24: 329418.
180. Vlhinen, M.,, P. Ollikka,, J. Niskamem,, P. Meyer,, I. Suominen,, M. Karp,, L. Holm,, J. Knowles,, and P. Mäntsälä. 1990. Site-directed mutagenesis of a thermostable α-amylase from Bacillus stearothermophilus: putative role of three conserved residues. J. Biochem. 107:267272.
181. Vlrolle, M.J.,, C. M. Long,, S. Chang,, and M. J. Bibb. Cloning, characterisation and regulation of an α-amylase gene from Streptomyces venezuelae. Gene 74:321334.
182. von Heijne, G.,, and L. Abrahmsen. 1989. Species-specific variation in signal peptide design. FEBS Lett. 244:439446.
183. Wachlnger, G.,, K. Bronnenmeier,, W. L. Staudenbauer,, and H. Schrempf. 1989. Identification of mycelium-associated cellulase from Streptomyces reticuli. Appl. Environ. Microbiol. 55:26532657.
184. Wakim, J.,, M. Robinson,, and J. A. Thoma. 1969. The active site of porcine pancreatic alpha amylase factors contributing to catalysis. Carbohydr. Res. 10:487503.
185. Waldron, C. R., Jr., C. A. Becker-Vallone, and D. E. Eveleigh. 1986. Isolation and characterization of a cellulolytic actinomycete Microbispora bispora. Appl. Microbiol. Biotechnol. 24:477486.
186. Waldron, C. R., Jr., and D. E. Eveleigh. 1986. Sacchar-ification of cellulosics by Microbispora bispora. Appl. Microbiol. Biotechnol. 24:487492.
187. Wang, L.-F.,, and R. Doi. 1990. Complex character of senS, a novel gene regulating expression of extracellular protein genes of Bacillus subtilis. J. Bacteriol. 172: 19391947.
188.Watanabe, K., K. Chishiro, K. Kitamura, and Y. Suzuki. 1991. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-l,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem. 266:2428724294.
189.Watanabe, K., K. Kitamura, H. Iha, and Y. Suzuki. 1990. Primary structure of the oligo-l,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene. Eur. J. Biochem. 192:609620.
190. Wlrsel, S.,, A. Lachmund,, G. Wildhardt,, and E. Ruttkowski. 1989. Three α-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization. Mol. Microbiol. 3:314.
191. Wong, W. K. R.,, B. Gerhard, Z. M. Guo, D. G. Kilbum, R. A. J. Warren, and R. C. Miller, Jr. 1986. Characterization and structure of an endoglucanase gene cenA of Cellulomonas fimi. Gene 44:315324.
192. Yamane, K.,, Y. Hlrata,, T. Furusato,, H. Yamazaki,, and A. Nakayama. 1984. Changes in the properties and molecular weights of Bacillus subtilis M-type and N-type α-amylases resulting from a spontaneous deletion.J. Biochem. 96:18491858.
193. Yamane, K.,, and B. Maruo,. 1980. Bacillus subtilis α-amylase genes, p. 117123. In K. Sakaguchi, and M. Ouishi (ed.). Molecular Breeding and Genetics of Applied Microorganisms. Academic Press, Inc., New York.
194.Yamazakl, H., K. Ohmura, A. Nakayama, Y. Takeichi, K. Otozai, M. Yamasaki, G. Tamura, and K. Yamane. 1983. α-Amylase genes {amyR2 and amyE+) from an α-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences. J. Bacteriol. 156:327337.
195.Yang, M. Y., A. Galizzi, and D. Henner. 1983. Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucleic Acids Res. 11:237249.
196. Yoneda, Y. 1980. Increased production of extracellular enzymes by the synergistic effect of genes introduced into Bacillus subtilis by stepwise transformation. Appl. Environ. Microbiol. 39:274276.
197. Yoshimatsu, T.,, K. Ozaki,, S. Shikata,, Y. Ohta,, K. Koike,, S. Kawai,, and S. Ito. 1990. Purification and characterization of alkaline endo-I,4-β-gIucanases from alkalophilic Bacillus sp. KSM-635. J. Gen. Microbiol. 136:19731979.
198.Yuuki, T., T. Nomura, H. Tezuka, A. Tsuboi, H. Yama-gata, N. Tsukagoshi, and S. Udaka. 1985. Complete nucleotide sequence of a gene coding for heat- and pH-stable α-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying α-amylases deduced from the DNA sequences. J. Biochem. 98:11471156.
199. Zhou, J.,, T. Baba,, T. Takano,, S. Kobayoshl,, and Y. Aral. 1989. Nucleotide sequence of the maltotetraohydralase gene from Pseudomonas saccharophilia. FEBS Lett. 255:3741.
200. Zukowski, M. M., 1992. Production of commercially valuable products, p. 311337. In R. H. Doi, and M. McGIoughlin (ed.), Biology of Bacilli: Applications to Industry. Butterworth-Heinemann, Boston.

Tables

Generic image for table
Table 1

Subtilisins obtained from plasmid-bearing strains

Citation: Ferrari E, Jarnagin A, Schmidt B. 1993. Commercial Production of Extracellular Enzymes, p 917-937. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch62

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