Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Structural Identification and Proteolytic Effects of the Hatching Enzyme from Starfish Asterias amurensis

Author(s): Zhi Jiang Li and Sang Moo Kim

Affiliation: Department of Marine Food Science and Technology, Gangneung-Wonju National University, 7 Jukheon-gil, Gangneung 210-702, Republic of Korea.

Keywords: Collagen, deglycosylation, fibrinogen, proteolytic effect, starfish hatching enzyme.

Abstract:

Hatching enzyme (HE) is secreted from the blastula stage during fertilization and can cleave the egg membrane. The structural identification and proteolytic effects on the collagen and fibrinogen were investigated in this study. Approximate 20 kDa of Asn-linked oligosaccharides were attached to the HE. Five peptide fragments of the starfish HE were homogenous to those of the coat matrix protein of starfish Patiria pectinifera. Amino acids of the starfish HE consisted of mainly Leu (10.0%), Asp (12.5%), and Glu (12.8%). Collagenolytic and fibrinolytic activities of the starfish HE were weaker than those of collagenase and α-chymotrypsin. The degree values of hydrolysis for collagenase and α- chymotrypsin were significantly higher than those of HE in a dose- and time-dependent manner. The peptide mappings of the starfish HE on the collagenolysis (110.7, 84.7, and 20.8 kDa) and fibrinogenolysis (34, 30, and 29 kDa) were different from those of collagenase and α-chymotrypsin. Based on the proteolytic effects on the collagen and fibrinogen, the starfish hatching enzyme might have the potential application to remove the matrix composition in scar or keloid tissue.

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Article Details

VOLUME: 21
ISSUE: 7
Page: [631 - 638]
Pages: 8
DOI: 10.2174/0929866521666140221153026