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κ-卡拉胶对猪肌原纤维蛋白凝胶特性调控机制的研究

Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan.

作者信息

Chen Zhi, Luo Cheng, Wang Kangxu, Chen Yinji, Zhuang Xinbo

机构信息

College of Biological Science and Agriculture, Qiannan Normal University for Nationalities, Duyun 558000, China.

College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, China.

出版信息

Foods. 2023 Mar 29;12(7):1444. doi: 10.3390/foods12071444.

DOI:10.3390/foods12071444
PMID:37048265
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10094032/
Abstract

The purpose of this study is to explain the mechanism of porcine myofibrillar protein gel properties modulated by κ-carrageenan. The textural properties results showed that the stress at fracture of the composite gel with 0.4% κ-carrageenan had the highest value (91.33 g), which suggested that the 0.4% κ-carrageenan addition was the limitation. The strain at fracture was significantly reduced with κ-carrageenan addition. The composite gel with 0.4% κ-carrageenan had the lowest proportion of T22 (7.85%) and the shortest T21 relaxation time (252.81 ms). The paraffin section showed that the phase separation behavior of the composite gel transformed from single-phase behavior to dispersed phase behavior to bi-continuous phase behavior, and the ratio of CG/MP phase area significantly increased from 0.06 to 1.73. The SEM showed that the three-dimensional network of myofibrillar protein transformed from a loose structure to a compact structure to an unaggregated structure with κ-carrageenan addition. The myofibrillar protein network of the treatment with 0.4% κ-carrageenan had the highest DF value (1.7858) and lowest lacunary value (0.452). The principal component analysis was performed on the data of microstructure and textural properties, and the results showed that the dispersed phase behavior and moisture stabilization promoted the aggregation of myofibrillar protein and the composite gel had better water holding capacity and textural properties, while bi-continuous phase behavior hindered the aggregation of myofibrillar protein and the composite gel had worse water holding capacity and textural properties.

摘要

本研究的目的是解释κ-卡拉胶调节猪肌原纤维蛋白凝胶特性的机制。质地特性结果表明,添加0.4%κ-卡拉胶的复合凝胶的断裂应力值最高(91.33 g),这表明添加0.4%κ-卡拉胶是一个限度。添加κ-卡拉胶后,断裂应变显著降低。添加0.4%κ-卡拉胶的复合凝胶的T22比例最低(7.85%),T21弛豫时间最短(252.81 ms)。石蜡切片显示,复合凝胶的相分离行为从单相行为转变为分散相行为再到双连续相行为,CG/MP相面积比从0.06显著增加到1.73。扫描电子显微镜显示,随着κ-卡拉胶的添加,肌原纤维蛋白的三维网络从松散结构转变为致密结构再到未聚集结构。添加0.4%κ-卡拉胶处理的肌原纤维蛋白网络的DF值最高(1.7858),孔隙率值最低(0.452)。对微观结构和质地特性数据进行主成分分析,结果表明,分散相行为和水分稳定促进了肌原纤维蛋白的聚集,复合凝胶具有更好的保水能力和质地特性,而双连续相行为阻碍了肌原纤维蛋白的聚集,复合凝胶的保水能力和质地特性较差。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/466ff166af46/foods-12-01444-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/3f987155cce7/foods-12-01444-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/b6098128cdd9/foods-12-01444-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/c03beb8feae1/foods-12-01444-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/dc1611a7edda/foods-12-01444-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/466ff166af46/foods-12-01444-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/3f987155cce7/foods-12-01444-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/b6098128cdd9/foods-12-01444-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/c03beb8feae1/foods-12-01444-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/dc1611a7edda/foods-12-01444-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/11cc/10094032/466ff166af46/foods-12-01444-g005.jpg

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