Effects of Three Hydrophilic Colloids on the Properties of Phosphorylated Surimi-Crab Meat Mixed Gels

The effects of adding different amounts (0.1%, 0.2%, 0.3%, 0.4% and 0.5%) of psyllium husk powder (PHP), gellan gum (GG) or konjac glucomannan (KGM) on the properties of phosphorylated surimi-crab meat mixed gels (MG) were investigated. The gel properties were improved by adding a small amount (0.1%...

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Bibliographic Details
Main Author: ZHU Yajun, YE Tao, LU Yufeng, XIA Lizhi, LIU Songkun, LU Yaokun, JIANG Shaotong, LIN Lin, LU Jianfeng
Format: Article
Language:English
Published: China Food Publishing Company 2023-08-01
Series:Shipin Kexue
Subjects:
Online Access:https://www.spkx.net.cn/fileup/1002-6630/PDF/2023-44-16-009.pdf
Description
Summary:The effects of adding different amounts (0.1%, 0.2%, 0.3%, 0.4% and 0.5%) of psyllium husk powder (PHP), gellan gum (GG) or konjac glucomannan (KGM) on the properties of phosphorylated surimi-crab meat mixed gels (MG) were investigated. The gel properties were improved by adding a small amount (0.1%) of PHP or GG. With increasing addition level of hydrophilic colloids, phase separation occurred, so that the gel properties did not significantly change and even began to decrease. However, the addition of KGM had no significant effect on the breaking force or gel strength, and no phase separation was observed under laser scanning confocal microscopy (LSCM). The addition of PHP and GG increased the temperature at which G’ began to decrease, which was beneficial to the improvement of gel properties. The denaturation of myosin required higher temperature and less energy in the phosphorylated MG system with hydrophilic colloids, and temperature may become a major influential factor in the denaturation process. The overall structural stability of proteins in MG was enhanced by adding a small amount of PHP or KGM. However, PHP and GG had a destructive effect on actin. On the contrary, the addition of a small amount of KGM could increase the structural stability of actin, which may be unfavorable for the formation of gels. The interaction between myosin and actin in the MG system was conducive to enhancing the overall structural stability of proteins. The three hydrophilic colloids, especially GG, at an addition level of 0.1% was beneficial to the improvement of gel properties. The incorporation of hydrophilic colloids may be a novel strategy to improve the quality of phosphorylated MG.
ISSN:1002-6630