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Interaction between carrageenan/soy protein isolates and salt-soluble meat protein

Paper ID Volume ID Publish Year Pages File Format Full-Text
18810 43033 2016 7 PDF Available
Title
Interaction between carrageenan/soy protein isolates and salt-soluble meat protein
Abstract

•Combination of CAR/SPI increased the gel strength and water retention of SSMP.•The content of α-helix decreased and β-sheet increased in combined gel of CAR/SPI/SSMP.•Properties improvement of SSMP/SPI/CAR combined gel was not related to chemical reaction.

The effects of combined κ-carrageenan (CAR) and soy protein isolate (SPI) on gel strength, water loss, the rheological properties, particle size, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and Raman spectroscopy of salt soluble meat protein were evaluated. Combination of CAR/SPI increased gel strength and water retention of SSMP (salt-soluble meat protein), suggesting that molecular interaction may have occurred. However, no indications of specific molecular interactions were observed upon addition of stabilizing/destabilizing reagents. The results showed that hydrophobic force affected the water retention of salt soluble protein gel, and hydrogen bond significantly affected the formation of gel. The analysis of the Raman spectra showed that adding of combined CAR/SPI in SSMP decreased the content of α-helix and increased the content of β-sheet. SDS-PAGE did not show significant interactions between SSMP and CAR/SPI indicating that the property improvement of combined SSMP/SPI/CAR gel was not related to chemical reaction. Instead, physical rearrangement process and electrostatic attraction resulted from SPI, CAR and SSMP molecule could contribute to the gel quality improvement.

Keywords
Salt soluble meat protein; Carrageenan; Soy protein isolate; Rheology; Gel strength; Syneresis
First Page Preview
Interaction between carrageenan/soy protein isolates and salt-soluble meat protein
Publisher
Database: Elsevier - ScienceDirect
Journal: Food and Bioproducts Processing - Volume 100, Part A, October 2016, Pages 47–53
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering