Characterization of a novel SGNH-type esterase from Lactobacillus plantarum

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• 作者：Yonggyu Kim^a ; ^b ; ¹ ; Bum Han Ryu^a ; ^b ; ¹ ; Jimin Kim^a ; ¹ ; Wanki Yoo^a ; ^b ; Deu Rae An^a ; ^b ; Boo-Young Kim^a ; Sena Kwon^a ; Sojeong Lee^a ; Ying Wang^a ; Kyeong Kyu Kim^b ; T. Doohun Kim^a ; ^{doohunkim@sookmyung.ac.kr}
• 关键词：LpSGNH1 ; SGNH esterase ; Lactobacillus plantarum
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：96
• 期：Complete
• 页码：560-568
• 全文大小：2214 K
• 卷排序：96

文摘

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) from Lactobacillus plantarum WCFS1 was identified, functionally characterized, and immobilized for biotechnological applications. Homologs of LpSGNH1 are also found in many lactic acid bacteria (LAB) species. Biochemical features of LpSGNH1 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 make LpSGNH1 a great candidate for extensive industrial applications. Furthermore, cross-linked enzyme aggregates of LpSGNH1 (CLEA-LpSGNH1) displayed recycling ability and thermal stability compared to free LpSGNH1, which could be useful for industrial applications. This work highlights the importance of LpSGNH1 in the preparation of commercial compounds, and LpSGNH1 can be used as a model system of SGNH esterases in lactic acid bacteria.