Thermal adaptation of α-amylases: a review

Extremophiles

Volumn 18, Issue 6, 2014, Pages 937-944

  Hiteshi, Kalpana ^a   Gupta, Reena ^a  

^a HIMACHAL PRADESH UNIVERSITY   (India)

Author keywords

Adaptation; Amylase; Intramolecular interactions; Stability

Indexed keywords

AMYLASE; BACTERIAL PROTEIN; FUNGAL PROTEIN;

ADAPTATION; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; HEAT; METABOLISM; MOLECULAR GENETICS;

ADAPTATION, PHYSIOLOGICAL; ALPHA-AMYLASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; FUNGAL PROTEINS; HOT TEMPERATURE; MOLECULAR SEQUENCE DATA;

EID: 84937511426     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-014-0674-5     Document Type: Review

References (90)

1. Abdel-Fattah YR, Soliman NA, El-Toukhy NM, El-Gendy H, Ahmed RS (2013) Production, purification and characterization of thermostable α-amylase produced by Bacillus licheniformis isolate AI20. J Chem 2013:1–11
2. Abu EA, Ado SA, James DB (2005) Raw starch degrading amylase production by mixed culture of Aspergillus niger and Saccharomyces cerevisiae. Afr J Biotechnol 4:785–790
3. Aghajari N, Feller G, Gerday C, Haser R (1998) Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci 7:564–572
4. Aghajari N, Van Petegen F, Villeret V, Chessa JP, Gerday C, Haser R, Van Beeumeen J (2003) Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins Struct Funct Genet 50:636–647
5. Akpan I, Bankole MO, Adesmovo AM, Lantunde Data GO (1999) Production of amylase by Aspergillus niger using rice bran and agricultural material. Trop Sci 39:77–79
6. Alariya SS, Seth S, Gupta S, Gupta BL (2013) Amylase activity of a starch degrading bacteria isolated from soil. Arch Appl Sci Res 5:15–24
7. Arikan B (2008) Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from thermophilic Bacillus sp. isolate A3-15. Bioresour Technol 99:3071–3076
8. Arpigny JL, Lamotte J, Gerday C (1997) Molecular adaptation to cold of an Antarctic bacterial lipase. J Mol Catal B Enzym 3:29–35
9. Babu KR, Satyanarayan T (1995) α-Amylase production by thermophilic Bacillus coagulans in solid state fermentation. Process Biochem 30:305–309
10. Benjamin S, Smitha RB, Jisha VN, Pradeep S, Priji P, Unni KN, Sarath Josh MK (2013) A monograph on amylases from Bacillus spp. Adv Biosci Biotechnol 4:227–241
11. Bordbar AK, Omidiyan K, Hosseinzadeh R (2005) Study on interaction of alpha amylase from Bacillus subtilis with cetyl trimethyl ammonium bromide. Biointerfaces 40:67–71
12. Cambillau C, Claverie JM (2000) Structural and genomic correlates of hyperthermostability. J Biol Chem 275:32383–32386
13. Chakravarty S, Vardarajan R (2000) Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett 470:65–69
14. Cipolla A, D’Amico S, Barumandzadeh R, Matagne A, Feller G (2011) Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium. J Biol Chem 286:38348-38355
15. Cipolla A, Delbrassine F, Da Lage J, Feller G (2012) Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride dependent alpha-amylases. Biochimie 94:1943–1950
16. D’Amico S, Gerday C, Feller G (2003) Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold adapted α-amylase. J Mol Biol 332:981–988
17. Daba T, Kojima K, Inouye K (2013) Interaction of wheat β-amylase with maltose and glucose as examined by fluorescence. J Biochem 2013:1–8
18. De Backer M, McSweeney S, Rasmussen HB, Riise BW, Lindley P, Hough E (2002) The 1.9A crystal structure of heat-labile shrimp alkaline phosphatase. J Mol Biol 318:1265–1274
19. De Moraes LMP, Astolfi Filho S, Ulhao CJ (1999) Purification and some properties of an amylase glucoamylase fusion protein from Saccharomyces cerevisiae. World J Microbiol Biotechnol 15:561–564
20. De Souza PM, Magalhaes PO (2010) Application of microbial α-amylase in industry—a review. Braz J Microbiol 41:850–861
21. Deb P, Talukdar SA, Mohsina K, Sarkar PK, Sayem SMA (2013) Production and partial characterization of extracellular amylase enzyme from Bacillus amyloliquefaciens P-001. Springer Plus 2:154
22. Declerck N, Machius M, Joyet P, Wiegand G, Huber R, Gaillardin C (2002) Engineering the thermostability of Bacillus licheniformis α-amylase. Biologia 57:203–211
23. Feller G (2010) Protein stability and enzyme activity at extreme biological temperatures. J Phys: Condens Matter 220:323101
24. Feller G (2013) Psychrophilic enzymes: from folding to function and biotechnology. Scientifica 2013:1–28
25. Feller G, Gerday C (1997) Psychrophilic enzymes: molecular bases of cold adaptation. Cell Mol Life Sci 53:830–841
26. Feller G, Gerday C (2003) Psychrophilic enzyme: hot topics in cold adaptation. Nat Rev Microbiol 1:200–208
27. Feller G, Payan F, Theys F, Qian M, Haser R, Gerday C (1994) Stability and structural analysis of α-amylase from Antarctic psychrophile Alteromonas haloplanctis A23. Eur J Biochem 222:441–447
28. Fincan SA, Enez B (2013) Production, purification, and characterization of thermostable a-amylase from thermophilic Geobacillus stearothermophilus. Starch 65:1–8
29. Fogarty WM, Kelly CT (1980) Amylases, amyloglucosidases and related glucanases. In: Rose AH (ed) Microbial enzymes and bioconversion, 4th edn. Academic Press, London, pp 115–170
30. Gerday C, Feller G (1997) Psychrophilic enzymes: a thermodynamic challenge. Biochim Biophys Acta 1342:119–131
31. Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B (2003) Microbial α-amylases: a biotechnological perspective. Process Biochem 38:1599–1616
32. Hailemarium AT, Gezmn TB, Haki GD (2013) Thermostable alpha amylase from geothermal sites of Ethiopia (Afar Region): isolation, purification and characterization. Green J Biol Sci 3:61–73
33. Haki GD, Rakshit SK (2003) Developments in industrially important thermostable enzymes: a review. Bioresour Technol 89:17–34
34. Hmidet N, Bayoudh A, Berrin JG, Kanoun S, Juge N, Nasri M (2008) Purification and biochemical characterization of a novel α-amylase from Bacillus licheniformis NH1: cloning, nucleotide sequence and expression of amy N gene in Escherichia coli. Process Biochem 43:499–510
35. Hwang KY, Song HK, Chang C, Lee J, Lee SY, Kim KK, Choe S, Sweet RM, Suh SW (1997) Crystal structure of thermostable alpha amylase from Bacillus licheniformis refined at 1.7 A resolution. Mol Cells 7:251–258
36. Iulek J, Franco OL, Silva M, Slivinski CT, Bloch CJ, Rigden DJ, Grossi-de-Sa´ MF (2000) Purification, biochemical characterization and partial primary structure of a new α-amylase inhibitor from Secale cereale (rye). Int J Biochem Cell Biol 32:1195–1204
37. Jaenicke R (1991) Protein stability and molecular adaptations to extreme conditions. Eur J Biochem 202:715–728
38. Janecek A, Balaz A (1992) Alpha amylases and approach leading to their enhanced stability. FEBS Lett 304:1–3
39. Jenecek S, Svensson B, Henrissat B (1997) Domain evolution in the α-amylase family. J Mol Evol 45:322–331
40. 8-barrel domain and evolutionary relationship to other amylolytic enzymes. J Prot Chem 12:791–805
41. Joseph B, Ramteke PW, Thomas G (2008) Cold active microbial lipase; some hot issues and recent developments. Biotechnol Adv 26:457–470
42. Kachan AV, Evtushenkov AN (2013) Thermostable mutant variants of Bacillus sp. 406 α-amylase generated by site-directed mutagenesis. Cent Eur J Biol 2013:346–356
43. Karshikoff A, Ladenstein R (2001) Ion pairs and the thermotolerance of protein for hyperthermophiles: a “traffic rule” for hot roads. Trends Biochem Sci 26:550–556
44. Khalil A (2011) Isolation and characterization of three thermophilic bacterial strains (lipase, cellulase and amylase producers) from hot springs in Saudi Arabia. Afr J Biotechnol 10:8834–8839
45. Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho YJ (1999) Structural basis for cold adaptation. Sequence, biochemical properties and crystal structure for malate dehydrogenase from psychrophile Aquaspirillium arcticum. J Biol Chem 274:11761–11767
46. Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946–950
47. Kuddus M, Roohi (2010) Microbial cold active α-amylases: From fundamental to recent developments. Curr Res Technol Edu Topics Appl Microbiol Microb Biotechnol 2010:1265–1276
48. Kuddus M, Roohi, Arif JM, Ramteke PW (2011) An overview of cold-active microbial α-amylase: adaptation strategies and biotechnological potentials. Biotechnology 10:246–258
49. Kumar P, Satyanarayana T (2009) Microbial glucoamylases: characteristics and applications. Crit Rev Biotechnol 29:225–255
50. Kumar L, Awasthi G, Singh B (2011) Extremophile: a novel source of industrially important enzymes. Biotechnology 10:121–135
51. Kuriki T, Hondoh H, Matsuura Y (2005) The conclusive proof that supports the concept of the α-amylase family: structural and common catalytic mechanism. Biologia 60:13–16
52. Lakshmi HP, Prasad UV, Yeswanth S, Swarupa V, Prasad OH, Narasu ML, Gurunadha PV, Sarma K (2013) Molecular characterization of α-amylase from Staphylococcus aurius. Bioinformation 9:281–285
53. Leloup V, Colona P, Buleon A (1994) Bioconversion of cereal products. Godon Ed. VCH, New York, pp 79–127
54. Leveque E, Janacek S, Haye B, Belarbi A (2000) Thermophilic archeal amylolytic enzymes. Enzyme Microb Technol 26:13–14
55. Loladze VV, Ibarra-Molero B, Sanchez-Ruiz JM, Makhatadze GI (1999) Engineering a thermostable protein via optimization of charge–charge interactions on the protein surface. Biochem 38:16419–16423
56. MacGregor EA (1988) α-Amylase structure and activity. J Protein Chem 7:399–415
57. Michelin M, Silva T, Bennasi V, Juliana M (2010) Purification and characterization of thermostable amylase produced by the fungus Paecilomyces variotti. Carbohydr Res 345:2348–2353
58. Morita RY (1975) Psychrophilic bacteria. Bacteriol Rev 39:144–167
59. Muralikrishna G, Nirmala M (2005) Cereal α-amylase—an overview. Carbohydr Polym 60:163–173
60. Nam ES, Ahn JK (2011) Isolation and characterization of cold adapted bacteria producing lactose hydrolyzing enzyme isolated from soils of Nome area in Alaska. Int Res J Microbiol 2:348–355
61. Olaniyi OO, Akinyele BJ, Arotupin DJ (2010) Purification and characterization of beta amylase from Volvariella volvacea. Nig J Microbiol 24:1976–1982
62. Olufunke FT, Azeez II (2013) Purification and characterization of beta-amylase of Bacillus subtilis isolated from Kolanut Weevil. J Bio Life Sci 4:68–78
63. Ominyi Matthias C (2013) Optimization of α-amylase and glucoamylase production from three fungal strains isolated from Abakaliki, Ebonyi State. Eur J Exp Biol 3:26–34
64. Pandey A, Nigam P, Soccol CR, Soccol VT, Singh D, Mohan R (2000) Advances in microbial amylases. Biotechnol Appl Biochem 31:135–152
65. Peixoto SC, Jorge JA, Terenzi HF, Lourdes M, Polizeli TM (2003) Rhizopus microsporus var. rhizopodiformis: a thermotolerant fungus with potential for production of thermostable amylases. Int Microbiol 6:269–273
66. Perl D, Mueller U, Heinemann U, Schmid FX (2000) Two exposed amino acid residues confer thermostability on a cold shock protein. Nat Struct Biol 7:380–383
67. Rani T, Takagi T, Toda H (2007) Bacterial and mold amylases. In: Boyer P (ed) The enzymes. Academic Press Inc., New York, pp 235–271
68. Ray RR (2000) Purification and characterization of extracellular β-amylase of Bacillus megaterium B6. Acta Microbio Immunol Hung 47:29–40
69. Reddy NS, Annapoora N, Sambawa RK (2003) An overview of the microbial alpha amylase family. Afr J Biotechnol 2:645–648
70. Reidhaar-Olson JF, Sauer RT (1990) Functionally acceptable substitutions in two alpha-helical regions of lambda repressor. Proteins 7:306–316
71. Roohi, Kuddus M, Ahmad IZ, Arif JM (2011) Production of Cold-active Extracellular α-Amylase by Newly isolated Microbacterium foliorum GA2 from Gangotri glacier, Wetern Himalaya, India. Asian J Biotechnol 2011:1–11
72. Rozzell JD (1999) Commercial scale bio catalysis myths and realities. Bioorg Medic Chem 7:2253–2261
73. Russell RJ, Gerike U, Danson MJ, Hough DW, Taylor GL (1998) Structural adaptations of the cold active citrate synthase from an Antarctic bacterium. Structure 6:351–361
74. Sapag A, Wouters J, Lambert C, de Loannes P, Eyzaguirre J, Depiereux E (2002) The endoxylanases from family 11: computer analysis of protein sequences reveals important structural and phylogenetic relationships. J Biotechnol 95:109–131
75. Shafiei M, Ziaee AA, Amoozegar MA (2011) Purification and characterization of an organic-solvent tolerant halophilic α-amylase from the moderately halophilic Nesternkonia sp. strain F. J Ind Microbiol Biotechnol 38:275–281
76. Siddiqui KS, Cavicchioli R (2006) Cold adapted enzymes. Annu Rev Biochem 75:403–433
77. 2Mbb. Int Res J Microbiol 2:96–103
78. Smalas AO, Heimstad ES, Hordvik A, Willasse NP, Male R (1994) Cold adaptation of enzymes; structural comparison between salmon and bovine trypsins. Proteins Struct Funct Genet 20:149–166
79. Spectar S, Wang M, Carp SA, Robblee J, Hendsch ZS, Fairman R, Tidor B, Raleigh DP (2000) Rational modification of protein stability by the mutation of charged surface residues. Biochemistry 39:872–879
80. Stetter KO (1999) In: Horikoshi K, Grant WD (eds) Extremophiles: microbial life in extreme environments. Wiley, New York, pp 1–24
81. Strop P, Mayo SL (2000) Contribution of surface salt bridges to protein stability. Biochemistry 39:1251–1255
82. Takano K, Tsuchimori K, Yamagata Y, Yutani K (2000) Contribution of salt bridges near the surface of a protein to the conformational stability. Biochemistry 39:12375–12381
83. Tateno T, Fukuda H, Kondo A (2007) Production of l-lysine from starch by Corynebacterium glutamicum displaying a-amylase on its cell surface. Appl Microbiol Biotechnol 74:1213–1220
84. Thoma JA, Spradlin JE, Dygert S (1971) Plant and animal amylases. In: Boyer PD (ed) The enzymes. Academic Press, New York, pp 115–189
85. Toyota E, Ng KK, Kuninaga S, Sekizaki H, Ituh K, Tanizowa K, James MN (2002) Crystal structure and nucleotide sequence of an anionic trypsin from chum salmon (Oncorhynchus keta) in comparison with Atlantic salmon (Salmo salar) and bovine trypsin. J Mol Biol 324:391–397
86. Tutino ML (2001) A novel replication element from an Antarctic plasmid as a tool for the expression of proteins at low temperature. Extermophiles 5:257–264
87. Vidyalakshmi R, Paranthaman R, Indhumathi J (2009) Amylase production on submerged fermentation by Bacillus spp. World J Chem 4:89–91
88. Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: sources, uses and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1–43
89. Windish WW, Mhatre NS (1965) Microbial amylase. In: Wayne WU (ed) Advances in applied microbiology. Academic Press, New York, pp 273–304
90. Zuber H (1988) Temperature adaptation of lactate dehydrogenase. Structural functional or genetic aspects. Biophys Chem 29:171–179