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Identification of a novel gelatinolytic metalloproteinase (GMP) in the body wall of sea cucumber (Stichopus japonicus) and its involvement in collagen degradation

Paper ID Volume ID Publish Year Pages File Format Full-Text
34737 45042 2013 7 PDF Available
Title
Identification of a novel gelatinolytic metalloproteinase (GMP) in the body wall of sea cucumber (Stichopus japonicus) and its involvement in collagen degradation
Abstract

•We first purified a gelatinolytic metalloproteinase (GMP) from sea cucumbers.•Its properties and sea cucumber collagen degradation were studied.•GMP shows superior degradation of collagen activity and even at 4 °C.•The involvement of GMP in the autolysis of sea cucumber is proposed.

Body wall that mainly consists of collagen and polysaccharides is the edible part of sea cucumber and is easy to go autolysis, while the proteinase(s) responsible for autolysis remains unclear. In the present study, a gelatinolytic metalloproteinase (GMP) from the body wall of sea cucumber Stichopus japonicus was purified to homogeneity by a combination of ammonium sulfate fractionation and chromatographic steps including DEAE-Sephacel, Sephacryl S-200, Q-Sepharose and Phenyl-Sepharose. The molecular mass of GMP as estimated by SDS-PAGE and gelatin zymography was 45 kDa. The enzyme revealed high activity at a slightly alkaline pH range (8.0–9.0) and the optimal temperature was at 40–45 °C. Metalloproteinase inhibitors, EDTA, EGTA, and 1,10-phenanthroline, almost completely suppressed the activity, whereas other proteinase inhibitors did not show any effect. Peptide mass fingerprinting of the enzyme obtained 3 peptide fragments with a total of 58 amino acid residues, which was 91.4% identical to an alkaline metalloprotease from Pseudomonas fluorescens, strongly suggesting it is a metalloproteinase. Divalent metal ion Ca2+ is essential for its activity, indicating it is a calcium-dependent metalloproteinase. Furthermore, GMP hydrolyzed collagen effectively at 37 °C and gradually even at 4 °C, suggesting its involvement in the autolysis of sea cucumber.

Keywords
Sea cucumber; Gelatin zymography; Purification; Gelatinolytic metalloproteinase; Peptide mass fingerprinting
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Identification of a novel gelatinolytic metalloproteinase (GMP) in the body wall of sea cucumber (Stichopus japonicus) and its involvement in collagen degradation
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issues 5–6, May–June 2013, Pages 871–877
Authors
, , , , , , ,
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