Domain C of thermostable α-amylase of Geobacillus thermoleovorans mediates raw starch adsorption

Applied Microbiology and Biotechnology

Volumn 98, Issue 10, 2014, Pages 4503-4519

  Mehta, Deepika ^a   Satyanarayana, T ^a  

^a UNIVERSITY OF DELHI   (India)

Author keywords

Geobacillus thermoleovorans; Raw starch hydrolysis; Starch binding domain; Starch saccharification; Thermostable amylase

Indexed keywords

ADSORPTION; AMINO ACIDS; AMYLASES; ENCODING (SYMBOLS); GELATION; GENE ENCODING; SACCHARIFICATION; THERMODYNAMICS;

EQUILIBRIUM PARAMETERS; GEOBACILLUS THERMOLEOVORANS; LANGMUIR-HINSHELWOOD KINETICS; PHYLOGENETIC ANALYSIS; RAW STARCH ADSORPTION; RAW STARCH HYDROLYSIS; STARCH BINDING DOMAIN; THERMOPHILIC BACTERIA;

STARCH;

AMYLASE; BACTERIAL ENZYME; GT AMYII PROTEIN; STARCH; UNCLASSIFIED DRUG; PROTEIN BINDING;

ADSORPTION; AMINO ACID; CATALYSIS; ENZYME ACTIVITY; HYDROLYSIS; PHYLOGENETICS; PROTEIN; THERMODYNAMICS; THERMOPHILIC BACTERIUM;

ADSORPTION; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; GEOBACILLUS THERMOLEOVORANS; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PROTEIN DOMAIN; THERMODYNAMICS; CHEMISTRY; ENZYMOLOGY; GEOBACILLUS; ISOLATION AND PURIFICATION; KINETICS; MAIZE; MANIHOT; METABOLISM; MOLECULAR WEIGHT; PH; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; TEMPERATURE;

BACTERIA (MICROORGANISMS); GEOBACILLUS THERMOLEOVORANS; MANIHOT ESCULENTA; ZEA MAYS;

ADSORPTION; ALPHA-AMYLASES; ENZYME STABILITY; GEOBACILLUS; HYDROGEN-ION CONCENTRATION; KINETICS; MANIHOT; MOLECULAR WEIGHT; PHYLOGENY; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STARCH; TEMPERATURE; THERMODYNAMICS; ZEA MAYS;

EID: 84900831002     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5459-8     Document Type: Article

References (38)

1. Abe A, Tonozuka T, Sakano Y, Kamitori S (2004) Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 1 with maltoligosaccharides demonstrate the role of domain N acting as a starch binding domain. J Mol Biol 335:811-822 (Pubitemid 38352822)
2. Asoodeh A, Chamanic JK, Lagzian M (2010) A novel thermostable, acidophilic alpha-amylase from a new thermophilic "Bacillus sp. Ferdowsicous" isolated from Ferdows hot mineral spring in Iran: purification and biochemical characterization. Int J Biol Macromol 46:289-297
3. Bai Y, Huang H, Meng K, Shi P, Yang P, Luo H, Luo C, Feng Y, Zhang W, Yao B (2012) Identification of an acidic α-amylase from Alicyclobacillus sp. A4 and assessment of its application in the starch industry. Food Chem 131:1473-1478
4. Boraston AB, Healey M, Klassen J, Ficko-Blean E, van Bueren AL, Law V (2006) A structural and functional analysis of α-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J Biol Chem 281:587-598 (Pubitemid 43671222)
5. Bǒzić N, Ruiz J, Lopez-Santin J, Vujčić Z (2011) Production and properties of the highly efficient raw starch digesting α-amylase from a Bacillus licheniformis ATCC 9945a. Biochem Eng J 53:203-209
6. Bozonnet S, Jensen MT, Nielsen MM, Aghajari N, Jensen MH, Kramhøft B, Willemoes M, Tranier S, Haser R, Svensson B (2007) The 'pair of sugar tongs' site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity. FEBS J 274:5055-5067 (Pubitemid 47481177)
7. Buedenbender S, Schulz GE (2009) Structural base for enzymatic cyclodextrin hydrolysis. J Mol Bio 385:606-617
8. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate-Active EnZymes (CAZy) database: an expert resource for glycogenomics. Nucleic Acids Res 37:D233-D238
9. Chai YY, Rahman RN, Illias RM, Goh KM (2012) Cloning and characterization of two new thermostable and alkalitolerant α-amylases fromthe Anoxybacillus species that produce high levels of maltose. J Ind Microbiol Biotechnol 39:731-741
10. Delano WL (2002) The PyMOL molecular graphics system. DeLano Scientific, San Carlos
11. Dheeran P, Kumar S, Jaiswal YK, Adhikari DK (2010) Characterization of hyperthermostable α-amylase from Geobacillus sp. IIPTN. Appl Microbiol Biotechnol 86:1857-1866
12. Ezeji TC, Bahl H (2006) Purification, characterization, and synergistic action of phytate-resistant alpha-amylase and alpha-glucosidase from Geobacillus thermodenitrificans HRO10. J Biotechnol 125:27-38 (Pubitemid 44082006)
13. Frillingos S, Linden A, Niehaus F, Vargas C, Nieto JJ, Ventosa A, Antranikian G, Drainas C (2000) Cloning and expression of alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in the moderately halophilic bacterium Halomonas elongata. J Appl Microbiol 88:495-503 (Pubitemid 30171485)
14. Fritzsche HB, Schwede T, Schulz GE (2003) Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92. Eur J Biochem 270:2332-2341 (Pubitemid 36605582)
15. Galvez A (2005) Analyzing cold enzyme starch hydrolysis technology in new ethanol plant design. Ethanol Producer 11:58-60
16. Guillén D, Santiago M, Linares L, Pérez R, Morlon J, Ruiz B, Sánchez S, Rodríguez-Sanoja R (2007) Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains. Appl Environ Microbiol 73:3833-3837
17. Hall KR, Eagleton LC, Acrivos A, Vermeulen T (1966) Pore- and solid-diffusion kinetics in fixed-bed adsorption under constant-pattern conditions. Ind Eng Chem Fund 5:212-223
18. 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 amyN gene in Escherichia coli. Proc Biochem 43:499-510
19. Hua YW, Chi MCH, Lo HF, Hsu WH, Lin LL (2004) Fusion of Bacillus stearothermophilus leucine aminopeptidase II with the raw starch binding domain of Bacillus sp. strain TS-23 α-amylase generates a chimeric enzyme with enhanced thermostability and catalytic activity. J Ind Microbiol Biotechnol 31:273-277
20. Iefuji H, Chino M, Kato M, Iimura Y (1996) Raw starch digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing. Biochem J 318:989-996
21. Janeček Š (2002) How many conserved sequence regions are there in the α-amylase family? Biologia. Bratislava 57(suppl 11):29-41
22. Karakas B, Inana M, Certel M (2010) Expression and characterization of Bacillus subtilis PY22 α-amylase in Pichia pastoris. J Mol Catal B Enzym 64(3-4):129-134
23. Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409:241-246
24. Lo H-F, Lin L-L, Chiang W-Y, Chie M-C, Hsu W-H, Chang C-T (2002) Deletion analysis of the C-terminal region of the α-amylase of Bacillus sp. strain TS-23. Arch Microbiol 178:115-123 (Pubitemid 34762252)
25. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265-275
26. Mehta D, Satyanarayana T (2013a) Biochemical and molecular characterization of recombinant acidic and thermostable raw starch hydrolysing α-amylase from an extreme thermophile Geobacillus thermoleovorans. J Mol Catal B Enzym 85-86:229-238
27. Mehta D, Satyanarayana T (2013b) Dimerization mediates thermoadaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans. PLoS One 8(9):1-13
28. Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 3:426-428
29. Mok S-C, Teh A-H, Saito JA, Najimudin N, Alam M (2013) Crystal structure of a compact α-amylase from Geobacillus thermoleovorans. Enzyme Microb Technol 53:46-54
30. Puspasari F, Radjasa OK, Noer AS, Nurachman Z, Syah YM, van der Maarel M, Dijkhuizen L, Janeček S, Natalia D (2013) Raw starch degrading α-amylase from Bacillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme. J Appl Microbiol 114:108-120
31. 2+ independent α-amylase of an extreme thermophile Geobacillus thermoleovorans. Appl Biochem Biotechnol 142:179-193
32. Robert X, Haser R, Gottschalk TE, Ratajczak F, Hugues D, Svensson B, Aghajari N (2003) The structure of barley α-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs. Structure 11:973-984 (Pubitemid 36966786)
33. Sorimachi K, Gal-Coëffet MFL, Williamson G, Archer DB, Williamson MP (1997) Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin. Structure 5:647-661
34. Sumitani J-I, Tottori T, Kawaguchi T, Arai M (2000) New type of starch binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 α-amylase contributes to starch binding and raw starch degrading. Biochem J 350:477-484
35. Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24:1596-1599
36. van Bueren AL, Boraston AB (2007) The structural basis of α-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima. JMol Biol 365:555-560 (Pubitemid 44960354)
37. Yadav JK (2013)Macromolecular crowding enhances catalytic efficiency and stability of α-amylase. doi: 10.5402/2013/737805
38. Yamaguchia R, Inoueb Y, Tokunagab H, Ishibashib M, Arakawac T, Sumitanid J-I, Kawaguchid T, Tokunaga M (2012) Halophilic characterization of starch binding domain from Kocuria varians α-amylase. Int J Biol Macromol 50:95-102