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Analysis, gene cloning and expression of two α-amylases from Bacillus cereus

Published online by Cambridge University Press:  30 October 2009

Zhang Lin-lin ,
Wang Qi ,
Li Rong-xi ,
Wang Yong-jun  and
Mei Ru-hong
Zhang Lin-lin
Affiliation:
Department of Plant Pathology, China Agricultural University, Beijing 100094, China Department of Agronomy, Inner Mongolia Agricultural University, Huhehaote 010018, China
Wang Qi*
Affiliation:
Department of Plant Pathology, China Agricultural University, Beijing 100094, China
Li Rong-xi
Affiliation:
Department of Agronomy, Inner Mongolia Agricultural University, Huhehaote 010018, China
Wang Yong-jun
Affiliation:
Department of Plant Pathology, China Agricultural University, Beijing 100094, China
Mei Ru-hong
Affiliation:
Department of Agronomy, Inner Mongolia Agricultural University, Huhehaote 010018, China
*
*Corresponding author. E-mail: wangqi@cau.edu.cn
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Abstract

Bacillus cereus can produce α-amylase, which has important industrial production value and can endure high temperatures. The enzymatic characteristics of two α-amylases from B. cereus (B905 and B904) were studied. The results showed that both preserved their activity at 90–100°C. Their thermal stability and enzymatic activity did not depend on Ca2+. However, their protein molecular weights were obviously different. The structural genes of amy905 and amy904 were cloned successfully using the polymerase chain reaction (PCR) and expressed in Escherichia coli. The amy904 and amy905 genes were 1362 bp and 1761 bp long and their protein molecular weights were about 55 kDa and 68 kDa, respectively.

Keywords

Bacillus cereusα-amylasegene clonegene expression
Type
Research Papers
Information
Chinese Journal of Agricultural Biotechnology , Volume 6 , Issue 2 , August 2009 , pp. 135 - 140
Copyright
Copyright © China Agricultural University 2009

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References

Deutch, CE (2002) Characterization of a salt-tolerant extracellular α-amylase from Bacillus dipsosauri. Letters in Applied Microbiology 35: 78–84.CrossRefGoogle ScholarPubMed
Du, BB and Hao, S (2006) Expression of a thermostable α-amylase mutant into Escherichia coli and Pichia pastoris. Acta Microbiologica Sinica 46(5): 827–830 (in Chinese with English abstract).Google ScholarPubMed
Guo, JQ and Li, YM (2006) Molecular cloning and expression of extremely thermostable and acid-stable amylase gene in Pichia pastoris. Chinese Journal of Biotechnology 22(2): 237–242 (in Chinese with English abstract).Google ScholarPubMed
Kang, HK and Lee, JH (2004) Cloning and expression of Lipomyces starkeyi alpha-amylase in Escherichia coli and determination of some of its properties. Microbiology Letters 233(1): 53–56.CrossRefGoogle ScholarPubMed
Kong, XL and Wang, JY (1989) Research and application of α-amylase. Microbiology 16(5): 282–287 (in Chinese with English abstract).Google Scholar
Li, JX and Cai, H (2004) Cloning expression of heat-stable α-amylase gene from Bacillus licheniformis in E. coli. Food and Fermentation Industries 1(30): 70–73 (in Chinese with English abstract).Google Scholar
MacGregor, EA and Janecek, S (2001) Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochimica et Biophysica Acta 1548: 1–20.Google Scholar
Niu, DD and Xu, M (2006) Cloning of the gene encoding a thermostable α-amylase from Bacillus licheniformis CICIM B0204 and functional identification of its promoter. Acta Microbiologica Sinica 46(4): 576–580 (in Chinese with English abstract).Google ScholarPubMed
Wang, LP and Peng, DK (2007) Construction of a highly effective expression system of Bacillus subtilis recombined xylanase gene. Journal of Agricultural Biotechnology 15(1): 133–137 (in Chinese with English abstract).Google Scholar
Xia, QCH (2002) The progress and development of proteomic research. Bulletin of the Chinese Academy of Sciences 17(3): 166–169 (in Chinese).Google Scholar
Zhang, YW and Zhang, ZY (2004) Cloning and expression in E. coli of cDNA encoding sweet potato β-amylase. High Technology Letters 14(9): 29–33 (in Chinese with English abstract).Google Scholar
Zhou, JC and Ma, XD (2006) A new method to identify α-amylase activity and its producing bacteria. Journal of Huazhong Agricultural University 6: 58–61 (in Chinese with English abstract).Google Scholar