Effect of molecular characteristics of Konjac glucomannan on gelling and rheological properties of Tilapia myofibrillar protein.

Autor: Jian W; Department of Medical Technology, Xiamen Medical College, Xiamen 361000, China; College of Food Science, South China Agricultural University, Guangzhou 510642, China. Electronic address: jianwenjie123@163.com., Wu H; Department of Medical Technology, Xiamen Medical College, Xiamen 361000, China., Wu L; Department of Medical Technology, Xiamen Medical College, Xiamen 361000, China., Wu Y; Department of Biotechnology, Xiamen Ocean Vocational College, Xiamen 361000, China., Jia L; College of Food Science and Technology,Shanghai Ocean University, Shanghai 201306, China., Pang J; College of Food Science, South China Agricultural University, Guangzhou 510642, China., Sun YM; College of Food Science, South China Agricultural University, Guangzhou 510642, China. Electronic address: ymsun@scau.edu.cn.
Jazyk: angličtina
Zdroj: Carbohydrate polymers [Carbohydr Polym] 2016 Oct 05; Vol. 150, pp. 21-31. Date of Electronic Publication: 2016 May 03.
DOI: 10.1016/j.carbpol.2016.05.001
Abstrakt: Konjac glucomannan (KGM) is an important gelling agent in composite gels. This study aimed to investigate the effects of KGM molecular characteristics (molecular weight, size and conformation) on gelling properties of Tilapia myofibrillar protein (TMP). In this work, TMP composite gels were prepared under neutral pH with varying KGM (native KGM, 10kGy-KGM, 20kGy-KGM, and 100kGy-KGM) of different molecular characteristics. Native KGM, 10kGy-KGM, and 20kGy-KGM exerted negative effect on gel strength or whiteness of TMP gels. Interestingly 100kGy-KGM improved gelling properties and whiteness of TMP gels. Such effects presented by varying KGM were attributed the physical filling behaviors and the interaction between KGM and TMP. These behaviors or interactions are resulted from different molecular size and conformation. Smaller molecular size (root-mean square radius, Rz 20.2nm) and approximated spherical conformation in 100kGy-KGM enhanced its interaction with TMP and maintained its compact and smooth structure, but the larger molecular size (Rz≥40.2nm) and random coil conformation in other KGMs inhibited part of actins from gelling and deteriorated the network structure. Our study provided principle knowledge to understand the structure-functions relationships of KGM-TMP composite gels. These results can be used to provide theoretical guidance for surimi gel processing.
(Copyright © 2016 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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