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Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)

Paper ID Volume ID Publish Year Pages File Format Full-Text
35859 45111 2007 7 PDF Available
Title
Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)
Abstract

Mullet (Mugil cephalus) muscle homogenates were adjusted to different pH ranging from 2 to12 and the proteins extracted were evaluated for changes in solubility and conformational characteristics viz. surface hydrophobicity and reactive sulphydryl groups. Altering the pH of muscle homogenate to acidic or alkaline increased protein solubility. The hydrophobicity of the proteins increased on exposure to extreme pH indicating unfolding. The reactive sulphydryl groups decreased at acidic and alkaline pH with the lowest at pH 4. When the pH of the muscle homogenates was brought back to the original pH (6.3), the protein solubility was found to decrease. Reactive sulphydryl groups and ANS hydrophobicity of the proteins increased on readjusting the pH resulting in a molten-globule state. The electrophortogram of the samples corresponded well with the observations. Alterations in functional properties of these modified proteins are an area of interest for commercial application.

Keywords
Fish muscle; pH; Solubility; Reactive sulphydryls; Surface hydrophobicity; SDS-PAGE
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Influence of pH on the solubility and conformational characteristics of muscle proteins from mullet (Mugil cephalus)
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 42, Issue 7, July 2007, Pages 1056–1062
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
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