文献类型：期刊文献

英文题名：Biodegradation of waste greases and biochemical properties of a novel lipase from Pseudomonas synxantha PS1

作者：Cai, Xianghai[1];Chen, Siqi[1];Yang, Hong[1];Wang, Wei[1];Lin, Lin[2];Shen, Yaling[1];Wei, Wei[1];Wei, Dong-zhi[1]

机构：[1]E China Univ Sci & Technol, Newworld Inst Biotechnol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China;[2]Natl Engn Res Ctr Nanotechnol, Res Lab Funct Nanomat, Shanghai 200241, Peoples R China

年份：2016

卷号：62

期号：7

起止页码：588

外文期刊名：CANADIAN JOURNAL OF MICROBIOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000378785100006)】；

基金：This research was financially supported by the National High Technology Research and Development Program of China (Nos. 2013AA102109 and 2012AA022206), the Fundamental Research Funds for the Central Universities of China (No. WF1214047), the National Natural Science Foundation of China (No. C050203-31200596), and the National Major Science and Technology Projects of China (No. 2012ZX09304009).

语种：英文

外文关键词：characterization; Pseudomonas synxantha; lipase; biodegradation

摘要：A lipase-producing bacterial strain was isolated from oil-well-produced water in Shengli oilfield (Shandong province, China) and was identified as Pseudomonas synxantha by 16S rDNA sequence analysis (named Pseudomonas synxantha PS1). Strain PS1 showed a maximum lipase activity of 10.8 U/mL after culturing for 48 h at 30 degrees C, with lactose (4 g/L) as carbon source, tryptone (8 g/L) as nitrogen source, olive oil (0.5%, v/v) as inductor, and the initial pH 8.0. Meanwhile, the lipase gene from P. synxantha PS1 was cloned and expressed in Escherichia coli BL21 with the vector pET28a. The novel gene (lipPS1) has an open reading frame of 1425 bp and encodes a 474 aa lipase (LipPS1) sharing the most identity (87%) with the lipase in Pseudomonas fluorescens. LipPS1 preferably acted on substrates with a long chain (C-10-C-18) of fatty acids. The optimum pH and temperature of the recombinant enzyme were 8.0 and 40 degrees C, respectively, towards the optimum substrate p-nitrophenyl palmitate. The LipPS1 showed remarkable stability under alkaline conditions and was stable at pH 7.0-10.0 (retaining more than 60% activity). From the organic solvents tests, the lipase was activated by 15% (v/v) methanol (112%), 15% ethanol (127%), and 15% n-butyl alcohol (116%). LipPS1 presented strong biodegradability of waste grease; 93% of waste grease was hydrolyzed into fatty acid after 12 h at 30 degrees C. This is the first report of the lipase activity and lipase gene obtained from P. synxantha (including wild strain and recombinant strain) and of the recombinant LipPS1 with the detailed enzymatic properties. Also a preliminary study of the biodegradability of waste greases shows the potential value in industry applications.