A novel cold-adapted beta-galactosidase from Alteromonas sp. ML117 cleaves milk lactose effectively at low temperature
文献类型： 外文期刊
作者： Yao, Congyu 1 ; Sun, Jingjing 1 ; Wang, Wei 1 ; Zhuang, Zhiwei 4 ; Liu, Junzhong 1 ; Hao, Jianhua 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fishery, Minist Agr & Rural Affairs, Qingdao 266071, Shandong, Peoples R China
2.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, Qingdao 266071, Shandong, Peoples R China
4.New Hope Liuhe Co Ltd, Qingdao 266071, Shandong, Peoples R China
5.Jiangsu Collaborat Innovat Ctr Exploitat & Utiliz, Lianyungang 222005, Peoples R China
关键词： Alteromonas; Cold-adapted enzyme; beta-galactosidase; Enzyme properties; Lactose hydrolysis
期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）
ISSN： 1359-5113
年卷期： 2019 年 82 卷
页码：
收录情况： SCI
摘要： A novel beta-galactosidase gene (Bgal) was cloned from the marine bacterium Alteromonas sp. ML117. Bgal from Alteromonas sp. ML117 was heterologously expressed in Escherichia coli BL21 (DE3) cells to study the enzymatic properties of the recombinant beta-galactosidase. Using gel-filtration chromatography and SDS-PAGE, the recombinant enzyme was identified to be a tetrameric enzyme that belonged to the glycoside hydrolase family GH2. The purified recombinant Bgal was able to hydrolyze lactose and o-nitrophenyl-beta-D-galactopyranoside (ONPG), and showed maximum activity at pH 8.0 and 30 degrees C to hydrolyze ONPG and at 35 degrees C to hydrolyze lactose. The enzyme's activity level quickly diminished when incubated at 35 degrees C, suggesting that it was a cold-adapted variant. At 10 degrees C, the purified enzyme had K-m values of 1.6 mM for ONPG and 3.8 mM for lactose. The enzyme tolerated NaCl, and retained 80% of its activity in a 30% ethanol reaction system. In addition, the recombinant Bgal hydrolyzed 86% of the lactose from milk over 24 h at 10 degrees C. Taken together, this study identified a recombinant Alteromonas sp. ML117 beta-galactosidase that may be used for industrial applications.
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