Journal
BIORESOURCE TECHNOLOGY
Volume 104, Issue -, Pages 518-522Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2011.09.112
Keywords
Phospholipase B; Gene cloning; Expression; Pseudomonas fluorescens; Escherichia coli
Funding
- Major Projects on Control and Rectification of Water Body Pollution [2008ZX07207-003]
- Major State Basic Research Development Program of China (973 Program) [2007CB714300]
- National High Technology Research and Development Program of China (863 Program) [2009AA02Z202]
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A gene from Pseudomonas fluorescens BIT-18 encoding a protein with phospholipase B activity (Pf-PLB) was cloned in E. coli BL21 (DE3). The open reading frame consists of 1272 bp and potentially encodes a protein of 423 amino acid residues with a calculated molecular mass of 45.8 kDa. The nucleotide sequence of Pf-PLB is 45%, 42%, 41%, 40%, 33%, and 31% identical to that of Bifidobacterium animals, Mycobacterium parascrofulaceum, Acidobacterium capsulatum, Lactobacillus johnsonii, Moraxella bovis, and Moraxella catarrhalis, respectively. The His-tagged protein was purified by affinity chromatography and the eluted protein hydrolyzed both the 1- and 2-ester bond of phosphatidylcholine. The recombinant Pf-PLB had optimal activity at pH 6.0 and 30 degrees C, and it showed 20.1% higher efficiency in the conversion rate of the phosphorus content than the wild-type. (C) 2011 Elsevier Ltd. All rights reserved.
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