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白木通籽分离蛋白的理化与功能性质研究
引用本文:白木通籽分离蛋白的理化与功能性质研究[J]. 食品工业科技, 2012, (23): 76-80. DOI: 10.13386/j.issn1002-0306.2012.23.075
作者姓名:史卿  杜研学  赵强  阮霞  熊华  钟红兰  白春清  黄声芳
作者单位:南昌大学食品科学与技术国家重点实验室,江西南昌,330047
基金项目:江西省科技计划项目(20122BBF60061);南昌大学食品科学与技术国家重点实验室目标导向项目(SKLF-MB-201005);江西省重大招标项目-茶油绿色高效加工及质量安全技术研究与示范(赣科发2010[217]号)
摘    要:以白木通籽为原料,采用碱提酸沉法,制备白木通籽分离蛋白(API),并对其理化性质与功能性质进行了分析。结果表明:白木通籽分离蛋白含17种氨基酸,其中谷氨酸和天门冬氨酸的含量相对较高,有贮藏蛋白的共性。苏氨酸为白木通籽分离蛋白的第一限制性氨基酸。通过SDS-PAGE分析,白木通籽分离蛋白的亚基分子量范围为25~35ku。圆二色性光谱分析表明,白木通籽分离蛋白的二级结构主要由β-折叠和无规则卷曲组成,含量分别为31.2%和36.6%。白木通籽分离蛋白的等电点在pH4~5之间,在此pH范围内,蛋白的溶解性和起泡能力均最低。 

关 键 词:白木通籽分离蛋白    理化性质    功能性质  
收稿时间:2012-06-18

Physicochemical and functional properties of protein isolate extracted from Akebia trifoliata var. australis seed
Physicochemical and functional properties of protein isolate extracted from Akebia trifoliata var. australis seed[J]. Science and Technology of Food Industry, 2012, (23): 76-80. DOI: 10.13386/j.issn1002-0306.2012.23.075
Authors:SHI Qing  DU Yan-xue  ZHAO Qiang  RUAN Xia  XIONG Hua   ZHONG Hong-lan  BAI Chun-qing  HUANG Sheng-fang
Affiliation:(State Key Laboratory of Food Science and Technology,Nanchang University,Nanchang 330047,China)
Abstract:Akebia trifoliata var. australis seed protein isolate (API) was prepared using the methods of alkali extraction and acid precipitation. The physicochemical and functional properties of API were characterized. The results showed that API contained 17 kinds of amino acids. Glutamic acid and aspartic acid were the most abundant amino acids in API, consistent with most storage proteins. With respect to nutritional parameter, threonine was found as the first limiting amino acids for API. From the analysis of SDS-PAGE, molecular weights of API were from 25. 0 ~ 35. 0ku. Accounting for 31. 2% and 36. 6%. β-strand and random coil were found to be the major secondary structures in API. The isoelectric point of API was between 4 and 5. Protein solubility and the foaming capacity were minimal at that pH values.
Keywords:Akebia trifoliata var.australis seed protein isolate  physicochemical properties  functional properties
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