数字农科院2.0

Ultrastructure Of Longissimus Dorsi Myofibrillar P.roteins And Heat-Induced Gels A s Observed With Atomic Force Microscopy: Effects Of Ph Values And Sodium Ions

文献类型： 外文期刊

作者： Wang, WT; Pan, T; Zhang, YQ; Wang, Y; Zhu, J; Zhang, DQ

作者机构：

关键词： Atomic force microscopy; gel; myofibrillar proteins; roughness; ultrastructure

期刊名称： INTERNATIONAL JOURNAL OF FOOD PROPERTIES

ISSN： 1094-2912

年卷期： 2019 年 22 卷 1 期

页码：

收录情况： JCR（2021版） ; EI（2021版）

摘要： Water holding capacity, texture characteristics, and qualitative structural properties had been mainly focused on heat-induced gelation of myofibrillar proteins; however, the quantitative analysis to ultrastructure of the proteins and heat-induced gel was rarely reported in the previous study. The objective of this study was to investigate quantitatively the effects of different pH values and ion concentrations on the ultrastructure of myofibrillar proteins and thermal-induced gel from swine longissimus dorsi using atomic force microscopy. Protein and gel groups in different conditions were set up, respectively, for the comparative study. The proteins of the gel group were treated first by water and 0.1 M, 0.3 M, 0.6 M NaCl solutions separately at pH 5.5, 6.5, 7.5, and then heated in the water bath. However, protein group were treated without the water bath but directly dried in the air at room temperature. Image roughness Rq were used as an index for quantitative analysis. Atomic force microscopy and related offline analysis software were used to collect the height images and determine the roughness of the myofibrillar proteins and heat-induced gel, respectively. It had been indicated that pH values and ionic concentrations had shown a significant effect on the roughness of heat-induced gel and myofibrillar proteins according to the atomic force microscopy (AFM) height images. The roughness of the gel is minimal while the myofibrillar proteins were treated by 0.6 M NaCl at pH 7.5. It is suggested that roughness of AFM height images could be used as an index to determine the gelling conditions.

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