Abstract：
:The mature ARM lipase gene was cloned into the pTrcHis expression vector and over-expressed in Escherichia coli TOP10 host. The optimum lipase expression was obtained after 18 h post induction incubation with 1.0mM IPTG, where the lipase activity was approximately 1623-fold higher than wild type. A rapid, high efficient, one-step purification of the His-tagged recombinant lipase was achieved using immobilized metal affinity chromatography with 63.2% recovery and purification factor of 14.6. The purified lipase was characterized as a high active (7092 U mg(-1)), serine-hydrolase, thermostable, organic solvent tolerant, 1,3-specific lipase with a molecular weight of about 44 kDa. The enzyme was a monomer with disulfide bond(s) in its structure, but was not a metalloenzyme. ARM lipase was active in a broad range of temperature and pH with optimum lipolytic activity at pH 8.0 and 65°C. The enzyme retained 50% residual activity at pH 6.0-7.0, 50°C for more than 150 min.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Ebrahimpour A,Rahman RN,Basri M,Salleh ABdoi
10.1016/j.biortech.2011.03.083subject
Has Abstractpub_date
2011-07-01 00:00:00pages
6972-81issue
13eissn
0960-8524issn
1873-2976pii
S0960-8524(11)00440-8journal_volume
102pub_type
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