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Lipase fraction from the viscera of grey mullet (Mugil cephalus): Isolation, partial purification and some biochemical characteristics

Paper ID Volume ID Publish Year Pages File Format Full-Text
18367 42720 2007 9 PDF Available
Title
Lipase fraction from the viscera of grey mullet (Mugil cephalus): Isolation, partial purification and some biochemical characteristics
Abstract

A lipase was partially purified from the viscera of grey mullet (Mugil cephalus) by ammonium sulfate fractionation followed by simultaneous desalting and concentration by ultrafiltration, and affinity chromatography on cholate-EAH-Sepharose 4B. The partially purified grey mullet lipase (GML) was active within the pH range of 7–10, with an optimum pH of 8.0, and was stable from pH 4 to 10. The enzyme was active within the temperature range of 20–60 °C, and exhibited an optimum temperature for the hydrolysis of p-nitrophenyl palmitate at 50 °C, and was stable between 10 and 50 °C, beyond which it lost activity progressively. Based on the temperature activity data, the activation energy for the hydrolysis of p-NPP was calculated as 1.94 kcal/mol (8.15 kJ/mol). The p-nitrophenyl esters of medium to long chain fatty acid (C10–C16) served as good substrates for the enzyme and hydrolytic activity was enhanced by Mg2+, Mn2+, NaN3, and EDTA, but strongly inhibited by Hg2+, and Cu2+. Lower concentrations (25–10%, v/v) of water-miscible organic solvents (dimethyl sulfoxide, dimethyl formamide, iso-propanol, and methanol) had negligible effect on the activity of the lipase while higher concentrations (≥50%, v/v) completely inhibited enzyme activity. GML was remarkably stable in benzene, toluene, hexane, heptane, and iso-octane and was also activated by these solvents with hexane giving the most activation. Lower concentrations of trihydroxylated bile salts (sodium taurocholate, and sodium cholate) were more effective activators of GML than the dihydroxylated bile salt (sodium deoxycholate).

Keywords
Lipase; Enzyme purification; Stability; Enzyme activation
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Lipase fraction from the viscera of grey mullet (Mugil cephalus): Isolation, partial purification and some biochemical characteristics
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 40, Issue 3, 5 February 2007, Pages 394–402
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us