Bioprocessing of starch using enzyme technology

Food Biotechnology, Second Edition

Volumn , Issue , 2005, Pages 709-722

  Ravi Kumar, K ^a   Umesh Kumar, S ^a  

^a CENTRAL FOOD TECHNOLOGICAL RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85133994265     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (57)

1. Yamasaki, Y., Y. Suzuki, J. Ozawa. Three forms of A-glucosidase and a glucoamylase from Aspergillus awamori. Agric. Biol. Chem. 41:2149-2161, 1977.
2. Bhella, R.S., I. Altosaar. Production of multiple forms of glucoamylase in Aspergillus awamori. Biochem. Cell. Biol. 65:762-765, 1987.
3. Ramasesh, N., K.R. Sreekantiah, V.S. Murthy. Purification and characterization of a thermophilic A-amylase of Aspergillus niger van Tieghem. Starch 34:274-279, 1982.
4. Lineback, D.R., I.J. Russell, C. Rasmussen. Two forms of the glucoamylase of Aspergillus niger. Arch. Biochem. Biophys. 134:539-553, 1969.
5. Kita, A., H. Matsui, A. Somoto, A. Kimura, M. Takata, S. Chiba. Substrate specificity and subsite affinities of crystalline A-glucosidase from Aspergillus niger. Agric. Biol. Chem. 55:2327-2335, 1991.
6. Matsuura, Y., M. Kusonoki, W. Harada, M. Kakudo. Structure and possible catatlytic residues of Taka- amylaseA. J. Biochem. 95:697-702, 1984.
7. Saha, B.C., T. Mitsue, S. Ueda. Glucoamylase produced by submerged culture of Aspergillus oryzae. Starch 31:307-314, 1979.
8. Milner, J.A., J.D. Martin, A. Smith. Two-stage inocula for the production of alpha-amylase by Bacillus amyloliquefaciens. Enzyme Microbiol. Technol. 21:382-386, 1997.
9. Antrim, R.L., B.A. Solheim, L. Solheim, R. Meadows, A.L. Auterinen, J. Cunefare, S. Karppelin. A new Bacillus licheniformis alpha-amylase capable of low pH liquefaction. Starch 43:355-360, 1991.
10. Ogasahara, K., A. Imanishi, T. Isemura. Studies on thermophilic A-amylase from Bacilus stearothermophilus, I: some general and physico-chemical properties of thermophilic A-amy lase. J. Biochem. 67:65-75, 1970.
11. Ohdan, K., T. Kuriki, H. Kaneko, J. Shimada, T. Takada, Z. Fujimoto, H. Mizuno, S. Okada. Characteristics of two forms of A-amylases and structural implication. Appl. Environ. Microbiol. 65:4652-4658, 1999.
12. Brumm, P.J., R.E. Hebeda, W.M. Teague. Purification and characterization of the commercialized, cloned Bacillus megaterium A-amylase, part I: purification and hydrolytic properties. Starch 43:315-319, 1991.
13. Lappalainen, A., M.L. Nikupaavola, T. Suortti, K. Poutanen. Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification. Starch 43:477-182, 1991.
14. Hyun, H.H., J.G. Zeikus. General biochemical characterization of thermostable extracellular B-amylase from Clostridium thermosulfurogens. Appl. Environ. Microbiol. 49:1162-1167, 1985.
15. Monma, M., Y. Yamamoto, N. Kagei, K. Kainuma. Raw starch digestion by A-amylase and glucoamylase from Chalara paradoxa. Starch 41:382-385, 1989.
16. Sanoja, R.R., J. Morlon-Guyot, J. Jore, J. Pintado, N. Juge, J.P. Guyot. Comparative characterization of complete and truncated forms of Lactobacillus amylovorus A-amylase and role of the c-terminal direct repeats in raw-starch binding. Appl. Environ. Microbiol. 66:3350-3356, 2000.
17. Takahashi, K., A. Totsuka, T. Nakakuki, N. Nakamura. Production and application of a malto-genic amylase by a strain of Thermomonospora viridis TF-35. Starch 44:96-101, 1992.
18. Dubey, A.K., C. Suresh, R. Kavitha, N.G. Karanth, S. Umesh-Kumar. Evidence that the glucoamylases and A-amylase secreted by Aspergillus niger are proteolytically processed products of a precursor enzyme. FEBS Lett. 471:251-255, 2000.
19. Sakano, Y., M. Sano, T. Kobayashi. Hydrolysis of A-1,6 glucosidic linkages by A-amylases. Agric. Biol. Chem. 49:3041-3043, 1985.
20. Rosendal, P., B.H. Nielsen, N.K. Lange. Stability of bacterial alpha-amylase in the starch liquefaction process. Starch 31:368-372, 1979.
21. Kelly, C.T., W.M. Fogarty. Microbial alkaline enzymes. Process. Biochem. 11(6):3-9, 1976.
22. Klibanov, A.M. Stabilization of enzymes against thermal inactivation. Adv. Appl. Microbiol. 29:1-28, 1983.
23. Chiang, J.P., J.E. Alter, M. Sternberg. Purification and characterization of a thermostable A-amylase from B. licheniformis. Starch 31:86-92, 1979.
24. Umesh-Kumar, S., F. Rehana, K. Nand. Production of an extracellular thermostable calcium-inhibited A-amylase by Bacillus licheniformis MY 10. Enzyme Microbiol. Technol. 12:714-716, 1990.
25. Rogers, J.C. Conserved amino acid sequence domains in A-amylases from plants, mammals and bacteria. Biochem. Biophys. Res. Commun. 128:470-476, 1985.
26. Hsiu, J., E.H. Fischer, E.A. Stein. A-Amylases as calcium-metalloenzymes, II: calcium and the catalytic activity. Biochemistry 3:61-66, 1964.
27. Toda, H., I. Kato, K. Narita. Correlation of the masked sulfhydryl group with the essential calcium in Taka-amylase A. J. Biochem. 63:295-301, 1968.
28. Vihinen, M., P. Mantsala. Microbial amylolytic enzymes. Critic. Rev. Biochem. Mol. Biol. 24:329-418, 1989.
29. Fogarty, W.M., C.T. Kelly. Amylases amyloglucosidases and related glucanases. In: Microbial Enzymes and Bioconversions: Economic Microbiology, Rose, A.H., ed., New York: Academic Press, 1980, pp 115-170.
30. Dubey, A.K. Genetic improvement of A. niger for the production of a novel starch hydrolysing enzyme. Ph.D. Thesis, University of Mysore, India, 1999.
31. Boel, E., I. Hjort, B. Svensson, F. Norris, K.E. Norris, N.P. Fill. Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs. EMBO J. 3:1097-1102, 1984.
32. Boel, E., M.T. Hansen, I. Hjort, J. Hoegh, N.P. Fill. Two different types of intervening sequences in the glucoamylase gene from Aspergillus niger. EMBO J. 3:1581-1585, 1984.
33. Svensson, B., K. Larsen, A. Gunnarsson. Characterization of a glucoamylase G2 from Aspergilus niger. Eur. J. Biochem. 154:497-502, 1986.
34. Olsen, K., U. Christensen, M.R. Sierks, B. Svensson. Reaction mechanisms of Trp 120: Phe and wild type glucoamylases from A. niger interactions with maltooligodextrins and acarbose. Biochemistry 32:9686-9693, 1993.
35. Ly, H.D., S.G. Withers. Mutagenesis of glycosidases. Annu. Rev. Biochem. 68:487-522, 1999.
36. Chiba, S. Molecular mechanism in A-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem. 61:1233-1239, 1997.
37. Robyt, J., D. French. Purification and action pattern of an amylase from B. polymyxa. Arch. Biochem. Biophys. 104:338-345, 1964.
38. Maitin, V., R. Kavitha, S. Umesh-Kumar. Properties of extracellular amylase purified from a Bacillus species. World J. Microbiol. Biotechnol. 17:823-826, 2001.
39. Urlaub, H., G. Wober. Identification of isoamylase a glycogen-debranching enzyme from Bacillus amyloliquefaciens. FEBS Lett. 57:1-4, 1975.
40. Norman, B.E. A novel debranching enzyme for application in the glucose syrup industry. Starch 34:340-346, 1982.
41. Saha, B.C., J.G. Zeikus. Biotechnology of maltose syrup production. Process. Biochem. 22:78-82, 1987.
42. Bucke, C. Glucose-transforming enzymes. In: Microbial Enzymes and Biotechnology, Fogarty, W.M., ed., London: Applied Science, 1983, pp 93-129.
43. Boyce, C.O.L. Novo's Hand Book of Practical Biotechnology. Copenhagen: Novo industries A/S, 1986, pp 35-41.
44. Innis, M.A., M.J. Holland, P.C. McCabe, G.E. Cole, V.P. Wittman, R. Tal, K.W.K. Watt, D.H. Gelfand, J.P. Holland, J.H. Meade. Expression glycosylation and secretion of an Aspergillus glucoamylase by Saccharomyces cerevisiae. Science 228:21-26, 1985.
45. Svensson, B., M. Soggard. Protein engineering of amylases. Biochem. Soc. Trans. 20:34-42, 1992.
46. Tomazic, S.J., A. Klibanov. Why is one Bacillus A-amylase more resistant against irreversible thermoinactivation than another? J. Biol. Chem. 263:3092-3096, 1988.
47. Suzuki, Y., N. Ito, T. Yuuki, H. Yamagata, S. Udaka. Amino acid residues stabilizing a Bacillus A-amylase against irreversible thermoinactivation. J. Biol. Chem. 264:18933-18938, 1989.
48. Gottschalk, T.E., H.P. Fierobe, E. Mirgorodskaya, A.J. Clarke, D. Tull, B.W. Sigurskjold, T. Christensen, N. Payre, T.P. Frandsen, N. Juge, K.A. McGuire, S. Cottaz, P. Roepstorff, H. Driguez, G. Williamson, B. Svensson. Structure function and protein engineering of starch-degrading enzymes. Biochem. Soc. Trans. 26:198-204, 1998.
49. Fang, T.Y., P.M. Coutinho, P.J. Reilly, C. Ford. Mutations to alter A. awamori glucoamylase selectivity, I: Tyr 48 Phe 49→Trp, Tyr 116→Trp, Tyr 175→Phe, Arg 241→Lys, Ser 411→Ala and Ser 411→Gly. Protein Eng. 11:119-126, 1998.
50. Fang, T.Y., R.B. Honzatko, P.J. Reilly, C. Ford. Mutations to alter A. awamori glucoamylase selectivity, II: mutations at positions 119 and 121. Protein Eng. 11:127-133, 1998.
51. Liu, H.L., P.M. Coutinho, C. Ford, P.J. Reilly. Mutations to alter A. awamori glucoamylase selectivity, III: Asn 20-Cys/Ala 27-Cys/Ala 27-Pro, Ser 30-Pro, Lys 108-Met, Gly 137-Ala, 311-314 loop, Tyr 312-Trp and Ser 436-Protein Eng. 11:389-398, 1998.
52. Liu, H.L., C. Ford, P.J. Reilly. Mutations to alter A. awamori glucoamylase selectivity, IV: Asn 20-Cys/Ala 27-Cys, Ser 30-Pro, Gly 137-Ala, 311-314 loop, Ser 411-Ala and Ser 436-Protein Eng. 12:163-172, 1999.
53. Chen, H.M., Y. Li, T. Panda, F.U. Buehler, C. Ford, P.J. Reilly. Effect of replacing helical Glycine residues with alanines on reversible and irreversible stability and production of A. awamori glucoamylase. Protein Eng. 9:499-505, 1996.
54. Reilly, P.J. Protein engineering of glucoamylase to improve industrial performance: a review. Starch 51:269-274, 1999.
55. Leveque, E., S. Janecek, B. Haye, A. Belarbi. Thermophilic archeal amylolytic enzymes. Enzyme Microbiol. Technol. 26:3-14, 2000.
56. Ashikari, T., N. Nakamura, Y. Tanaka, N. Kiuchi, Y. Shibano,T. Tanaka, T. Amachi, H. Yoshizumi. Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast. Agric. Biol. Chem. 50:957-964, 1986.
57. Beaujean, A., C. Ducrocq-Assaf, R.S. Sangwan, G. Lilius, L. Bulow, B.S. Sangwan-Norreel. Engineering direct fructose production in processed potato tubers by expressing a bifunctional A-amylase/glucose isomerase gene complex. Biotechnol. Bioeng. 70:9-16, 2000.