Abstract:
:The gene encoding a cold-adapted phospholipase A(1) (PLA(1)) from a psychrotrophic, glacier soil bacterium Serratia sp. xjF1 was cloned by two-step PCR (general PCR and TAIL-PCR). The full-length fragment comprised two open reading frames plA and plS. The gene product of plA encoding 320 amino acids with a molecular weight of 33.8kDa was identified as a phospholipase A(1). Its amino acid sequence exhibited the highest homology to PLA(1) of Serratia marcescens (71%). plS encoded a protein of 251 amino acids, which showed no enzymatic activity. The result of plA expression in Escherichia coli indicated that plS might improve the efficient expression of PLA(1) in E. coli. Furthermore, PLA(1) was functionally expressed in Pichia pastoris, yielding 41.8U/mL in a 3.7L fermentor. The purified recombinant phospholipase A(1) (rPLA(1)) had features typical of cold-adapted enzymes with a temperature optimum of 35°C and a maximum activity of 70% at 10°C. The rate of catalysis was optimal at pH 9.0 and the enzyme could be slightly activated by Ca(2+). This is the first report on gene isolation and expression of cold-adapted PLA(1).
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Fu J,Huang H,Meng K,Yuan T,Yao B,Shi Y,Ouyang Pdoi
10.1016/j.enzmictec.2007.09.004subject
Has Abstractpub_date
2008-01-01 00:00:00pages
187-94issue
2eissn
0141-0229issn
1879-0909pii
S0141-0229(07)00310-9journal_volume
42pub_type
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