高强度超声对酸诱导乳清蛋白凝胶凝胶性能的影响。
Effects of high intensity ultrasound on acid-induced gelation properties of whey protein gel.
机构信息
Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China; Department of Food Science, Northeast Agriculture University, Harbin 150030, China; Department of Nutrition and Food Sciences, College of Agriculture and Life Sciences, University of Vermont, Burlington, VT 05405, USA.
出版信息
Ultrason Sonochem. 2017 Nov;39:810-815. doi: 10.1016/j.ultsonch.2017.05.039. Epub 2017 May 30.
Pre-heated whey protein isolate (WPI) solution (10% w/v, 85°C for 30min) was prepared and subjected to high-intensity ultrasound (HUS, 20kHz) at different durations (5-40min) before acidification to determine the effects of HUS on glucono-δ-lactone (GDL)-induced gelation properties of whey protein gel. Results showed that HUS reduced the particle size and increased surface free sulfhydryl groups of pre-heated whey protein solution. Free sulfhydryl (-SH) content of the acid-induced WPI gels (GIWG) and protein solubility in presence of 8M urea were significantly reduced (P<0.05) by HUS (20 or 40min), indicating that HUS facilitated formation of more disulfide bonds during/after the gelation process. HUS significantly increased (P<0.05) the water holding capacity (WHC), gel strength, gel firmness (G') as well as the frequency dependence of GIWG. The WHC, gel strength and gel firmness were positively correlated with surface free -SH content of pre-heated WPI and negatively correlated with particle size of pre-heated WPI and free -SH content of GIWG. The results indicated that high intensity ultrasound could be used for modifying whey protein to improve its gelling properties.
将预热的乳清蛋白分离物（WPI）溶液（10％w/v，85°C 加热 30min）进行预处理，并在酸化之前用高强度超声（HUS，20kHz）处理不同的时间（5-40min），以确定 HUS 对乳清蛋白凝胶的戊二醛（GDL）诱导的凝胶化性质的影响。结果表明，HUS 降低了预热乳清蛋白溶液的粒径并增加了表面游离巯基的含量。HUS（20 或 40min）显著降低了酸诱导的 WPI 凝胶（GIWG）中的游离巯基（-SH）含量和 8M 尿素存在下的蛋白质溶解度，表明 HUS 在凝胶化过程中/之后促进了更多二硫键的形成。HUS 显著增加了（P<0.05）持水力（WHC）、凝胶强度、凝胶硬度（G'）以及 GIWG 的频率依赖性。WHC、凝胶强度和凝胶硬度与预热 WPI 的表面游离 -SH 含量呈正相关，与预热 WPI 的粒径和 GIWG 的游离 -SH 含量呈负相关。结果表明，高强度超声可用于修饰乳清蛋白以改善其胶凝性质。
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