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Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3

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Abstract

By constructing the genomic library, a β-glucosidase gene, with a length of 2,382 bp, encoding 793 amino acids, designated bgla, is cloned from a marine bacterium Aeromonas sp. HC11e-3. The enzyme is expressed successfully in the recombinant host Escherichia coli BL21 (DE3) and purified using glutathione affinity purification system. It shows the optimal activity at pH 6, 55 °C and hydrolyzes aryl-glucoside specially. Ca2+, Mn2+, Zn2+, Ba2+, Pb2+, Sr2+ can activate the enzyme activity, whereas SDS, EDTA, DTT show slight inhibition to the enzyme activity. Homologous comparing shows that the enzyme belongs to glycosyl hydrolase family 3, exhibiting 46 % identity with a fully characterized glucosidase from Thermotoga neapolitana DSM 4359. Such results provide useful references for investigating other glucosidases in the glycosyl family 3 as well as developing glucosidases using in suitable industrial area.

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References

  • Arevalo VM, Ubeda IJF, Gundllapalli SB, Cordero ORR, Briones PAI (2006) Characterization of an exocellular [beta]-glucosidase from Debaryomyces pseudopolymorphus. Enzyme Microb Technol 39:229–234

    Article  Google Scholar 

  • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195–201

    Article  CAS  Google Scholar 

  • Belancic A, Gunata Z, Vallier MJ, Agosin E (2003) β-glucosidase from the grape native yeast Debaryomyces vanrijiae: purification, characterization, and its effect on monoterpene content of a muscat grape juice. J Agric Food Chem 51:1453–1459

    Article  CAS  Google Scholar 

  • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem 72:248–259

    Article  CAS  Google Scholar 

  • Butters TD (2007) Gaucher disease. Curr Opin Chem Biol 11, 412–418

    Google Scholar 

  • Chen S, Hong Y, Shao Z, Liu Z (2010) A cold-active β-glucosidase (Bgl1C) from a sea bacteria Exiguobacterium oxidotolerans A011. World J Microbiol Biotechnol 8:1427–1435

    Article  Google Scholar 

  • Eberhart B, Cross D, Chase L (1964) β-glucosidase system of Neurospora crassai: β-glucosidase and cellulase activities of mutant and wild-type strains. J Bacteriol 87:761–770

    CAS  Google Scholar 

  • Fan HX, Miao LL, Liu Y, Liu HC, Liu ZP (2011) Gene cloning and characterization of a cold-adapted [beta]-glucosidase belonging to glycosyl hydrolase family 1 from a psychrotolerant bacterium Micrococcus antarcticus. Enzyme Microb Technol 49:94–99

    Article  CAS  Google Scholar 

  • Feng Y, Dual CJ, Liu L, Tang JL, and Feng JX (2009) Properties of a metagenome-derived β-glucosidase from the contents of rabbit cecum. Biosci Biotechnol Biochem 73:1470–1473

    Google Scholar 

  • Harnpicharnchai P, Champreda V, Sornlake W, Eurwilaichitr L (2009) A thermotolerant [beta]-glucosidase isolated from an endophytic fungi, Periconia sp., with a possible use for biomass conversion to sugars. Protein Expr Purif 67:61–69

    Article  CAS  Google Scholar 

  • Janda JM (1991) Recent advances in the study of the taxonomy, pathogenicity, and infectious syndromes associated with the genus Aeromonas. Clin Microbiol Rev 4:397–410

    CAS  Google Scholar 

  • Janda JM, Abbott SL (2010) The genus Aeromonas: taxonomy, pathogenicity, and infection. Clin Microbiol Rev 23:35–73

    Article  CAS  Google Scholar 

  • Joo AR, Jeya M, Lee KM, Sim WI, Kim JS, Kim IW, Kim YS, Oh DK, Gunasekaran P, Lee JK (2009) Purification and characterization of a β-1, 4-glucosidase from a newly isolated strain of Fomitopsis pinicola. Appl Microbiol Biotechnol 83:285–294

    Article  CAS  Google Scholar 

  • Kennedy J, Marchesi JR, Dobson ADW (2008) Marine metagenomics: strategies for the discovery of novel enzymes with biotechnological applications from marine environments. Microb Cell Fact 7:27

    Google Scholar 

  • Ketudat CJR, Esen A (2010) β-Glucosidases. Cell Mol Life Sci 67:3389–3405

    Article  Google Scholar 

  • Leah R, Kigel J, Svendsen I, Mundy J (1995) Biochemical and molecular characterization of a barley see glucosidase d-. J Biol Chem 270:15789–15797

    Article  CAS  Google Scholar 

  • Lee KH, Piao HL, Kim HY, Choi SM, Jiang F, Hartung W, Hwang I, Kwak JM, Lee IJ (2006) Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid. Cell 126:1109–1120

    Article  CAS  Google Scholar 

  • Mao X, Hong Y, Shao Z, Zhao Y, Liu Z (2009) A novel cold-active and alkali-stable β-glucosidase gene isolated from the marine bacterium Martelella mediterranea. Appl Biochem Biotechnol 162:2136–2148

    Article  Google Scholar 

  • Morant AV, Jorgensen K, Jorgensen C, Paquette SM, Sanchez-Perez R, Moller BL, Bak S (2008) [beta]-Glucosidases as detonators of plant chemical defense. Phytochemistry 69:1795–1813

    Article  CAS  Google Scholar 

  • Patrick S, Blakely GW, Houston S, Moore J, Abratt VR, Bertalan M, Cerdeno-Tarraga AM, Quail MA, Corton N, Corton C (2010) Twenty-eight divergent polysaccharide loci specifying within-and amongst-strain capsule diversity in three strains of Bacteroides fragilis. Microbiology 156:3255–3269

    Article  CAS  Google Scholar 

  • Pozzo T, Pasten JL, Karlsson EN, Logan DT (2010) Structural and functional analyses of [beta]-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3. J Mol Biol 397:724–739

    Article  CAS  Google Scholar 

  • Qin Y, Zhang Y, He H, Zhu J, Chen G, Li W, Liang Z (2010) Screening and Identification of a fungal β-glucosidase and the enzymatic synthesis of gentiooligosaccharide. Appl Biochem Biotechnol 163:1012–1019

    Article  Google Scholar 

  • Shen Y, Zhang Y, Ma T, Bao X, Du F, Zhuang G, Qu Y (2008) Simultaneous saccharification and fermentation of acid-pretreated corncobs with a rEcombinant Saccharomyces cerevisiae expressing [beta]-glucosidase. Bioresour Technol 99:5099–5103

    Article  CAS  Google Scholar 

  • Shipkowski S, Brenchley JE (2005) Characterization of an unusual cold-active {beta}-glucosidase belonging to family 3 of the glycoside hydrolases from the psychrophilic isolate Paenibacillus sp. Strain C7. Appl Environ Microbiol 71:4225–4232

    Article  CAS  Google Scholar 

  • Turner P, Svensson D, Adlercreutz P, Karlsson ENA (2007) Novel variant of Thermotoga neapolitana [beta]-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation. J Biotechnol 130:67–74

    Article  CAS  Google Scholar 

  • Zhao G, Duan C, Pang H, Feng Y, Xu Y, Mo X, Xin Mo, Tang J, Feng J (2005) Cloning and identification a β-glucosidase gene umbgl3A of uncultured bacteria from bovine rumen. Southwest Chin J Agric Sci 18:427–476

    Google Scholar 

Download references

Acknowledgments

This work was supported by grants from the National Natural Science Foundation of China (NO.u1170303) and the open project of state key laboratory of Huazhong Agricultrual University (ALM0810).

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Correspondence to Ziduo liu.

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Xiaoluo Huang and Yan Zhao contribute equally to the work.

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Huang, X., Zhao, Y., Dai, Y. et al. Cloning and biochemical characterization of a glucosidase from a marine bacterium Aeromonas sp. HC11e-3. World J Microbiol Biotechnol 28, 3337–3344 (2012). https://doi.org/10.1007/s11274-012-1145-8

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  • DOI: https://doi.org/10.1007/s11274-012-1145-8

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