Int. J. Mol. Sci. 2011, 12(11), 7609-7625; doi:10.3390/ijms12117609
Article

Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223

1 Department of Biotechnology, School of Bioscience & Bioengineering, South China University of Technology, Guangzhou 510006, Guangdong, China 2 College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, Guangdong, China 3 School of Chemistry and Chemical Engineering, South China University of Technology, Guangzhou 510640, Guangdong, China These authors contributed equally to this work.
* Authors to whom correspondence should be addressed.
Received: 27 September 2011; in revised form: 25 October 2011 / Accepted: 28 October 2011 / Published: 7 November 2011
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract: Experiments were carried out to investigate the effects of various factors on the activity and conformation of recombinant leucine aminopeptidase of Bacillus kaustophilus CCRC 11223 (BkLAP) and potential utilization of BkLAP in the hydrolysis of anchovy protein. Optimal temperature and pH of BkLAP were 70 °C and 8.0 in potassium-phosphate buffer, respectively, and the activity was strongly stimulated by Ni2+, followed by Mn2+ and Co2+. Conformational studies via circular dichroism spectroscopy indicated that various factors could influence the secondary structure of BkLAP to different extents and further induce the changes in enzymatic activity. The secondary structure of BkLAP was slightly modified by Ni2+ at the concentration of 1×10−4 M, however, significant changes on the secondary structures of the enzyme were observed when Hg2+ was added to the concentration of 1×10−4 M. The potential application of BkLAP was evaluated through combination with the commercial or endogenous enzyme to hydrolysis the anchovy protein. Results showed that combining the BkLAP with other enzymes could significantly increase the degree of hydrolysis and amino acid component of hydrolysate. In this regard, BkLAP is a potential enzyme that can be used in the protein hydrolysate industry.
Keywords: leucine aminopeptidase; biochemical properties; circular dichroism spectroscopy; Bacillus kaustophilus CCRC 11223; hydrolysis; anchovy

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MDPI and ACS Style

Shen, Y.; Wang, F.; Lan, D.; Liu, Y.; Yang, B.; Wang, Y. Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223. Int. J. Mol. Sci. 2011, 12, 7609-7625.

AMA Style

Shen Y, Wang F, Lan D, Liu Y, Yang B, Wang Y. Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223. International Journal of Molecular Sciences. 2011; 12(11):7609-7625.

Chicago/Turabian Style

Shen, Yanfei; Wang, Fanghua; Lan, Dongming; Liu, Yuanyuan; Yang, Bo; Wang, Yonghua. 2011. "Biochemical Properties and Potential Applications of Recombinant Leucine Aminopeptidase from Bacillus kaustophilus CCRC 11223." Int. J. Mol. Sci. 12, no. 11: 7609-7625.

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