Volume 19, Issue 130 (2022)                   FSCT 2022, 19(130): 213-226 | Back to browse issues page


XML Persian Abstract Print


Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Najafian L. Comparative Study on Physicochemical Properties of Catfish Sarcoplasmic and Myofibrillar Protein Hydrolysates Produced by Enzymatic Hydrolysis. FSCT 2022; 19 (130) :213-226
URL: http://fsct.modares.ac.ir/article-7-63368-en.html
Department of Food Science and Technology, Sari Branch, Islamic Azad University, Sari, Iran , najafian_5828@yahoo.com
Abstract:   (915 Views)
The present work aimed to study the effect of enzymatic hydrolysis of sarcoplastic and myofibrillar proteins from pangasius sutchi fish on the chemical compositions, the solubility, degree of hydrolysis (DH), peptide content and amino acid compositions was evaluated and their molecular weight recorded. The fish sarcoplasmic protein hydrolysates (SPHs) and myofibrillar protein hydrolysates (MPHs) were produced using three types of proteases: papain, alcalase and flavourzyme. Physicochemical properties of proteins and molecular weight were investigated. Results indicated that type of protease affected the degree of hydrolysis (DH), where all of the enzymes showed high rate of hydrolysis during the first hour, and then gradually decreased. The type of enzyme and the extent of the DH greatly influenced the amino acid residue composition and the molecular weight of the protein hydrolysates. Different amino acid composition of proteins and their hydrolysates was observed. The soluble protein and peptide content of hydrolysates significantly increased by the increase in time of incubation. The high amount of hydrophobic and aromatic amino acids in the SPH and MPH can enhance the biological activities of the peptides. Results suggest that the protein hydrolysates derived from patin may be used in functional food and supplements.
 
Full-Text [PDF 664 kb]   (291 Downloads)    
Article Type: Original Research | Subject: Proteins and bioactive peptides
Received: 2022/08/5 | Accepted: 2022/10/9 | Published: 2022/12/1

Add your comments about this article : Your username or Email:
CAPTCHA

Send email to the article author


Rights and permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.