کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1975570 1060637 2011 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of an intracellular lipase from pleopods of whiteleg shrimp (Litopenaeus vannamei)
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Purification and characterization of an intracellular lipase from pleopods of whiteleg shrimp (Litopenaeus vannamei)
چکیده انگلیسی

An intracellular lipase present in the whiteleg shrimp Litopenaeus vannamei was detected in pleopods. The lipase from pleopods was purified and characterized by biochemical and kinetic parameters. Purified intracellular lipase has a molecular mass of 196 kDa, the polypeptide is assembled by two monomers, 95.26 and 63.36 kDa. The enzyme lacks glycosylation, and it has an isoelectric point of 5.0. The enzyme showed the highest activity at a temperature range of 30–40 °C at pH 8.0–10.0. Activity was completely inhibited by tetrahydrolipstatin and diethyl p-nitrophenyl phosphate, suggesting that the intracellular lipase is a serine lipase. The lipase hydrolyzes short and long-chain triacylglycerides, as well as naphthol derivatives at comparable rates in contrast to other sources of lipases. Specific activity of 930 U mg−1 and 416.56 U mg−1 was measured using triolein and tristearin at pH 8.0 at 30 °C as substrates, respectively. The lipase showed a KM,app of 41.03 mM and kcat/KM,app ratio of 4.88 using MUF–butyrate as the substrate. The intracellular lipase described for shrimp has a potential role in hydrolysis of triacylglycerides stored as fat body, as has been shown in humans.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 158, Issue 1, January 2011, Pages 99–105
نویسندگان
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