首页> 外文期刊>Journal of the Science of Food and Agriculture >Pre-deamidation of soy protein isolate exerts impacts on transglutaminase-induced glucosamine glycation and cross-linking as well as properties of the products
【24h】

Pre-deamidation of soy protein isolate exerts impacts on transglutaminase-induced glucosamine glycation and cross-linking as well as properties of the products

机译:大豆分离蛋白的预脱酰胺作用对转谷氨酰胺酶诱导的氨基葡萄糖糖基化和交联以及产品性能产生影响

获取原文
获取原文并翻译 | 示例
           

摘要

BACKGROUNDTransglutaminase (TGase) induces protein glycation and cross-linking, but results in lower solubility and digestibility due to excessive cross-linking. Deamidation of soy protein isolate (SPI) by HCl converts glutamine residues, and provides less opportunity for the two reactions. Two deamidated SPI products (DSPI1 and DSPI2) were thus glucosamine-glycated and cross-linked, to clarify the effects of pre-deamidation on the two reactions and properties of the products.
机译:背景转谷氨酰胺酶(TGase)诱导蛋白质糖基化和交联,但由于过度交联而导致较低的溶解度和消化率。 HCl对大豆分离蛋白(SPI)脱酰胺可转化谷氨酰胺残基,为这两个反应提供较少的机会。因此,将两种脱酰胺的SPI产品(DSPI1和DSPI2)进行了氨基葡萄糖糖基化和交联,以阐明预脱酰胺对两种反应和产品性能的影响。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号