Characterization of a novel SGNH-type esterase from Lactobacillus plantarum.
Characterization of a novel SGNH-type esterase from Lactobacillus plantarum.
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DOI:
10.1016/j.ijbiomac.2016.12.061
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发表时间:
2017-03
影响因子:
8.2
通讯作者:
Yonggyu Kim;B. H. Ryu;Jimin Kim;Wanki Yoo;D. R. An;Boo-young Kim;Sena Kwon;Sojeong Lee;Ying Wang;Kyeong Kyu Kim;T. Doohun Kim
中科院分区:
文献类型:
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作者:
Yonggyu Kim;B. H. Ryu;Jimin Kim;Wanki Yoo;D. R. An;Boo-young Kim;Sena Kwon;Sojeong Lee;Ying Wang;Kyeong Kyu Kim;T. Doohun Kim
Lactic acid bacteria (LAB) are sources of a large variety of microbial ester hydrolases because they can produce a wide range of short-chain esters, phenolic alcohols, and fatty acids. Here, a novel SGNH-type esterase (LpSGNH1) fromLactobacillus plantarumWCFS1 was identified, functionally characterized, and immobilized for biotechnological applications. Homologs ofLpSGNH1 are also found in many lactic acid bacteria (LAB) species. Biochemical features ofLpSGNH1 were investigated using mass spectrometry, gel filtration chromatography, enzyme kinetics, fluorescence, and circular dichroism (CD) spectroscopy.LpSGNH1 were retained its activity under conditions that would be encountered during fermentations. Interestingly,LpSGNH1 exhibited the ability to act on a broad range of substrates including ketoprofen acetate, cefotaxime (CTX), and 7-aminocephalosporanic acid (7-ACA) as well as glucose pentaacetate, acetylxylan, and acetylalginate, which makeLpSGNH1 a great candidate for extensive industrial applications. Furthermore, cross-linked enzyme aggregates ofLpSGNH1 (CLEA-LpSGNH1) displayed recycling ability and thermal stability compared to freeLpSGNH1, which could be useful for industrial applications. This work highlights the importance ofLpSGNH1 in the preparation of commercial compounds, andLpSGNH1 can be used as a model system of SGNH esterases in lactic acid bacteria.