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Study on the protein fractions extracted from the muscle tissue of Pinctada martensii and their hydrolysis by pancreatin  ( SCI-EXPANDED收录 EI收录)   被引量:10

文献类型:期刊文献

英文题名:Study on the protein fractions extracted from the muscle tissue of Pinctada martensii and their hydrolysis by pancreatin

作者:Zheng, Huina[1];Zhang, Chaohua[1];Qin, Xiaoming[1];Gao, Jialong[1];Li, Tianyong[1]

机构:[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Key Lab Aquat Prod Adv Proc, Guangdong Higher Educ Inst, Zhanjiang 524025, Guangdong, Peoples R China

年份:2012

卷号:47

期号:10

起止页码:2228

外文期刊名:INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

收录:SCI-EXPANDED(收录号:WOS:000308639700025)、、EI(收录号:20123815449918)、Scopus(收录号:2-s2.0-84866161111)、WOS

基金:This work was supported by the special funds of Guangdong Province University's construction and quality engineering disciplines (Grant No: 1109240), the special funds of China's modern agricultural technology system (Grant No: CARS-48-07B) and the introduction of talent funds of Guangdong Ocean University (Grant No: 0912259).

语种:英文

外文关键词:Pancreatin hydrolysate; Pinctada martensii; salt-soluble protein; sodium dodecyl sulphate polyacrylamide gel electrophoresis; water-soluble protein

外文摘要:Pinctada martensii muscle proteins were separated into water-soluble, salt-soluble and insoluble protein fractions. The salt-soluble protein fraction was the most abundant, comprising approximately 66.3% of the protein, followed by the water-soluble and insoluble protein fractions in decreasing order. sodium dodecyl sulphate polyacrylamide gel electrophoresis profiles showed that 35- and 97-kDa peptides represented the highest proportions of the water-soluble and salt-soluble protein fractions, respectively. The three protein fractions contained high levels of flavourful amino acids (Glu, Asp, Ala and Lys), with the water-soluble protein fraction having the highest level (47.1%). The size exclusion chromatography profiles of the water-soluble and salt-soluble protein pancreatin hydrolysate demonstrated no significant differences in the molecular weight distributions in the >20 000, 500010 000 and 20005000 Da fractions, while those of the insoluble protein pancreatin hydrolysate were different. In conclusion, the results provided some basic information that would contribute to the utilisation of these protein fractions.

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