Secretory expression, characterization and docking study of glucose-tolerant β-glucosidase from B. subtilis

International Journal of Biological Macromolecules

Volumn 85, Issue , 2016, Pages 425-433

  Chamoli, Shivangi ^a   Kumar, Piyush ^b   Navani, Naveen Kumar ^b   Verma, Ashok Kumar ^a  

^a G B PANT UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY ROORKEE   (India)

Author keywords

Extracellular expression; Molecular docking; Thermostable glucose tolerant glucosidase

Indexed keywords

4 NITROPHENYL BETA DEXTRO GALACTOPYRANOSIDE; 4 NITROPHENYL BETA DEXTRO GLUCOPYRANOSIDE; 4 NITROPHENYL BETA DEXTRO XYLOPYRANOSIDE; BETA GLUCOSIDASE; CELLOBIOSE; DELTA GLUCONOLACTONE; DETERGENT; GLUCONOLACTONE; GLUCOSE; METAL ION; ORGANIC SOLVENT; PYRANOSIDE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; RECOMBINANT PROTEIN;

ALPHA HELIX; ARTICLE; BACILLUS SUBTILIS; BETA SHEET; BIOTECHNOLOGICAL PRODUCTION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME RELEASE; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; ESCHERICHIA COLI; GLUCOSE TOLERANCE; HETEROLOGOUS EXPRESSION; HYDROGEN BOND; HYDROPHOBICITY; INHIBITION CONSTANT; MOLECULAR CLONING; MOLECULAR DOCKING; NONHUMAN; OPEN READING FRAME; PH; PROTEIN EXPRESSION; STRUCTURAL HOMOLOGY; TEMPERATURE; TIM BARREL; AMINO ACID SEQUENCE; CHEMISTRY; DNA SEQUENCE; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BETA-GLUCOSIDASE; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; GLUCOSE; HYDROGEN-ION CONCENTRATION; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84954550850     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2016.01.001     Document Type: Article

References (44)

1. Juturu V., Wu J.C. Microbial xylanases: engineering, production and applications. Biotechnol. Adv. 2012, 30:1219-1227.
2. Beguin P., Aubert J.P. The biological degradation of cellulose. FEMS Microbiol. Rev. 1994, 13:25-58.
3. Henrissat B. Cellulases and their interaction with cellulose. Cellulose 1994, 1:169-196.
4. Zhang Y.H.P., Lynd L.R. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol. Bioeng. 2004, 88:797-824.
5. Murphy L., Bohlin C., Baumann M.J., Olsen S.N., Sorensen T.H., Anderson L., Borch K., Westh P. Product inhibition of five Hypocrea jecorina cellulases. Enzyme Microb. Technol. 2013, 52:163-169.
6. Ramani G., Meera B., Vanitha C., Rajendhran J., Gunasekaran P. Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization. J. Ind. Microbiol. Biotechnol. 2015, 42:553-565.
7. Xue R., Woodley J.M. Process technology for multi-enzymatic reaction systems. Bioresour. Technol. 2012, 115:183-195.
8. Li W., Zhang W.W., Yang M.M., Chen Y.L. Cloning of the thermostable cellulase gene from newly isolated Bacillus subtilis and its expression in Escherichia coli. Mol. Biotechnol. 2008, 40:195-201.
9. Neu H.C., Heppel L.A. The release of enzymes from Eschenchia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 1965, 240:3685-3692.
10. Kwon K.S., Lee J., Kang H.G., Hah Y.C. Detection of β-glucosidase activity in polyacrylamide gels with esculin as substrate. Appl. Environ. Microbiol. 1994, 60:4584-4586.
11. Neil J.P., David E.B., Emyr O., Isabel V., Jozef V.B., Mahalingeshwara K.B. Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus. Biochem. J. 2001, 353:117-127.
12. Huang X., Zhao Y., Dai Y., Wu G., Shao Z., Zeng Q. Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3. World J. Microbiol. Biotechnol. 2012, 28:3337-3344.
13. Lobley A., Whitmore L., Wallace B.A. DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 2002, 18:211-212.
14. Ly H.D., Withers S.G. Mutagenesis of glycosidases. Annu. Rev. Biochem. 1999, 68:487-522.
15. Allison S.D. Cheaters, diffusion and nutrients constrain decomposition by microbial enzymes in spatially structured environments. Ecol. Lett. 2005, 8:626-635.
16. Burns R.G., Wallenstein M.D. Microbial extracellular enzymes and natural and synthetic polymer degradation in soil: current research and future prospects. World Sci. Congr. 2010, 19:67-69.
17. Agrawal R., Satlewal A., Verma A.K. Development of a β-glucosidase hyperproducing mutant by combined chemical and UV mutagenesis. Biotechnology 2013, 3:381-388.
18. Slos P., Speck D., Accart N., Kolbe H.V., Schubnel D., Bouchon B., Bischoff R., Kieny M.P. Recombinant choleratoxin B subunit in Escherichia coli: high-level secretion, purification, and characterization. Protein Expr. Purif. 1994, 5:518-526.
19. Gupta S., Adlakha N., Yazdani S.S. Efficient extracellular secretion of an endoglucanase and a b-glucosidase in E. coli. Protein Expr. Purif. 2013, 88:20-25.
20. Luo Z., Zhang Y., Bao J. Extracellular secretion of β-glucosidase in ethanologenic E. coli enhances ethanol fermentation of cellobiose. Appl. Biochem. Biotechnol. 2014, 174:772-783.
21. Naz S., Ikram N., Rajoka M.I., Sadaf S., Akhtar M.W. Enhanced production and characterization of a beta-glucosidase from Bacillus halodurans expressed in Escherichia coli. Biochemistry (Mosc.) 2010, 75:513-525.
22. Liu D., Zhang R., Yang X., Zhang Z., Song S., Miao Y., Shen Q. Characterization of a thermostable β-glucosidase from Aspergillus fumigates Z5, and its functional expression in Pichia pastoris X33. Microb. Cell Fact. 2012, 11:25.
23. Lee J.M., Kim Y.R., Kim J.K., Jeong G.T., Ha J.C., Kong I.S. Characterization of salt-tolerant β-glucosidase with increased thermostability under high salinity conditions from Bacillus sp. SJ-10 isolated from jeotgal, a traditional Korean fermented seafood. Bioprocess Biosyst. Eng. 2015, 38:1335-1346.
24. Choi I.S., Wi S.G., Jung S.R., Patel D.H., Bae H.J. Characterization and application of recombinant β-glucosidase (BglH) from Bacillus licheniformis KCTC 1918. J. Wood Sci. 2009, 55:329-334.
25. Hashimoto W., Miki H., Nankai H., Sato N., Kawai S., Murata K. Molecular cloning of two genes for β-d-glucosidase in Bacillus sp. GL1 and identification of one as a gellan-degrading enzyme. Arch. Biochem. Biophys. 1998, 360:1-9.
26. Kuo L.C., Lee K.T. Cloning expression, and characterization of two β-glucosidases from isoflavone glycoside-hydrolyzing Bacillus subtilis natto. J. Agric. Food Chem. 2008, 56:119-125.
27. Zahoor S., Javed M.M., Aftab M.N., Haq I.U. Cloning and expression of β-glucosidase gene from Bacillus licheniformis into E. coli BL 21 (DE3). Biologia 2011, 66:213-220.
28. Cantarel B.L., Coutinho P.M., Rancurel C., Bernard T., Lombard V., Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 2009, 37:D233-D238.
29. Gruninger R.J., Gong X., Forster R.J., McAllister T.A. Biochemical and kinetic characterization of the multifunctional β-glucosidase/β-xylosidase/α-arabinosidase, Bgxa1. Appl. Microbiol. Biotechnol. 2014, 98:3003-3012.
30. Nam E.S., Kim M.S., Lee H.B., Ahn J.K. β-Glycosidase of thermus thermophilus KNOUC202: gene and biochemical properties of the enzyme expressed in Escherichia coli. Appl. Biochem. Microbiol. 2010, 46:515-524.
31. Cota J., Correa T.L.R., Damasio A.R.L., Diogo J.A., Hoffmam Z.B., Hoffmam W., Oliveira L., Prade R.A., Squina R.A. Comparative analysis of three hyperthermophilic GH1 and GH3 family members with industrial potential. N. Biotechnol. 2015, 32:13-20.
32. Singhania R.R., Patel A.K., Sukumaran R.K., Larroche C., Pandey A. Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production. Bioresour. Technol. 2013, 127:500-507.
33. Dotsenko G.S., Sinitsyna O.A., Hinz S.W., Wery J., Sinitsyn A.P. Characterization of a GH family 3b-glycioside hydrolase from Chrysosporium lucknowense and its application to the hydrolysis of β-glucan and xylan. Bioresour. Technol. 2012, 112:345-349.
34. Krisch J., Bencsik O., Papp T., Vágvölgyi C., TaKó M. Characterization of abglucosidase with transgalactosylation capacity from the zygomycete Rhizomucor miehei. Bioresour. Technol. 2012, 114:555-560.
35. Li G., Jiang Y., Fan X.J., Liu Y.H. Molecular cloning and characterization of a novel β-glucosidase with high hydrolyzing ability for soybean isoflavone glycosides and glucose-tolerance from soil metagenomic library. Bioresour. Technol. 2012, 123:15-22.
36. Saha B.C., Bothast R.J. Production purification, and characterization of a highly glucose-tolerant novel beta-glucosidase from Candida peltata. Appl. Environ. Microbiol. 1996, 62:3165-3170.
37. Saibi W., Gargouri A. Cellobiose dehydrogenase influences the production of S. microspora β-glucosidase. World J. Microbiol. Biotechnol. 2012, 28:23-29.
38. Seidle H.F., Allison S.J., George E., Huber R.E. Trp-49 of the family 3 β-glucosidase from Aspergillus niger is important for its transglucosidic activity: creation of novel b-glucosidases with low transglucosidic efficiencies. Arch. Biochem. Biophys. 2006, 455:110-118.
39. Geiger G., Furrer G., Funk F., Brandl H., Schulin R. Heavy metal effects on beta-glucosidase activity influenced by pH and buffer systems. J. Enzyme Inhib. 1999, 14(5):365-379.
40. Batra J., Mishra S. Organic solvent tolerance and thermostability of a β-glucosidase co-engineered by random mutagenesis. J. Mol. Catal. B: Enzym. 2013, 96:61-66.
41. Hong J., Tamaki H., Kumagai H. Unusual hydrophobic linker region of β-glucosidase (BGLII) from Thermoascus aurantiacusis required for hyper-activation by organic solvents. Appl. Microbiol. Biotechnol. 2006, 73:80-88.
42. Sanchez-Ruiz J.M. Protein kinetic stability. Biophys. Chem. 2010, 148:1-15.
43. Woody R.W., Dunker A.K. Circular Dichroism and the Conformational Analysis of Biomolecules 1996, 109-182. Plenum Press, New York. G.D. Fasman (Ed.).
44. Yamasaki M., Yano H., Aoki K. Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength. Int. J. Biol. Macromol. 1990, 12:263-268.