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高压处理对含 CaCl2 和 κ-卡拉胶的盐溶性肉蛋白凝胶特性的影响。

Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl2 and κ-carrageenan.

机构信息

School of Biology and Food Engineering, Hefei University of Technology, Hefei, Anhui, People's Republic of China.

出版信息

Meat Sci. 2013 Sep;95(1):22-6. doi: 10.1016/j.meatsci.2013.04.025. Epub 2013 Apr 16.

Abstract

The effects of high pressure processing (HPP) on the water-binding capacity and texture profile (TPA) of salt-soluble meat protein (SSMP) containing 0.2% CaCl2 and 0.6% κ-carrageenan (SSMP-CK) gels were investigated. The results showed that 300-400 MPa improved water-binding capacity and decreased TPA parameters of SSMP-CK gels (P<0.05), while 100 MPa could increase hardness and chewiness of the gels. The thermal transition temperature peak for the myosin head (Tpeak1) of SSMP disappeared on addition of CaCl2 and κ-carrageenan. 300 MPa produced a new peak, and caused a shift of the NH-stretching left peak and amide I and the disappearance of NH-stretching right peak. The destruction of network structure and the weakening of molecular interaction within the pressurized gels could result in the decrease of TPA parameters. Thus gelling properties could be modified by HPP, κ-carrageenan and Ca(2+). It is of interest to develop low-fat and sodium-reduced meat products.

摘要

研究了高压处理(HPP)对含 0.2%CaCl2 和 0.6%κ-卡拉胶(SSMP-CK)的盐溶性肉蛋白(SSMP)凝胶的结合水能力和质地剖面(TPA)的影响。结果表明,300-400 MPa 提高了 SSMP-CK 凝胶的结合水能力并降低了 TPA 参数(P<0.05),而 100 MPa 则增加了凝胶的硬度和咀嚼性。添加 CaCl2 和 κ-卡拉胶后,肌球蛋白头部(Tpeak1)的热转变温度峰值消失。300 MPa 产生了一个新的峰值,并导致 NH 伸缩左峰和酰胺 I 的移动以及 NH 伸缩右峰的消失。加压凝胶中网络结构的破坏和分子相互作用的减弱可能导致 TPA 参数的降低。因此,HPP、κ-卡拉胶和 Ca(2+)可以改变凝胶特性。开发低脂和低盐的肉类产品很有意义。

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