کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
70846 48849 2009 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Separation, characterization and catalytic properties of Lip2 isoforms from Candida sp. 99-125
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
Separation, characterization and catalytic properties of Lip2 isoforms from Candida sp. 99-125
چکیده انگلیسی

Lipase (EC.3.1.1.3) from Candida sp. 99-125 was separated into four isoforms (isoform A, isoform B, isoform C, and isoform D) by two steps of ion exchange chromatography. As analyzed on SDS- and non-denaturing PAGE, the four isoforms were homogenous and had the same molecular weight of approximate 38 kDa. MALDI-TOF peptide mass fingerprinting maps and circular dichroism spectra showed the isoforms had similar peptide patterns belonging to the same protein encoded by the YLlip2 gene and different secondary structures. The isoforms had a little distinct optimum temperature in the range of 20–35 °C, and the same optimum pH (8.0). They remained to be active in methanol, ethanol and ethylene glycol at the concentration of 10% and 20% (v/v) and acetone at the concentration of 10% (v/v), and sensitive to EDTA. Triton X-100, Sodium cholate and CHAPS slightly increased their activities. The metal ion Ca2+ and Mg2+ had mild effect on lipase activity. The isoforms showed a preference for long chain fatty acid triglyceride (triolein and olive). The lipase purified by one step of ion exchange chromatography and isoforms were less active than crude enzyme to catalyze cetyl alcohol and oleic acid in n-hexane, whereas the presence of small concentration of added water dramatically activated crude lipase but less the purified preparations.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 56, Issues 2–3, February 2009, Pages 115–121
نویسندگان
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