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中国精品科技期刊2020
刘颖, 刘丽宅, 于晓红, 付薇, 张丹, 窦博鑫. 限制性酶解乳清蛋白功能性质研究[J]. 食品工业科技, 2017, (04): 127-131. DOI: 10.13386/j.issn1002-0306.2017.04.016
引用本文: 刘颖, 刘丽宅, 于晓红, 付薇, 张丹, 窦博鑫. 限制性酶解乳清蛋白功能性质研究[J]. 食品工业科技, 2017, (04): 127-131. DOI: 10.13386/j.issn1002-0306.2017.04.016
LIU Ying, LIU Li- zhai, YU Xiao- hong, FU Wei, ZHANG Dan, DOU Bo- xin. Study on limited enzymatic hydrolysis of whey protein and functional properties[J]. Science and Technology of Food Industry, 2017, (04): 127-131. DOI: 10.13386/j.issn1002-0306.2017.04.016
Citation: LIU Ying, LIU Li- zhai, YU Xiao- hong, FU Wei, ZHANG Dan, DOU Bo- xin. Study on limited enzymatic hydrolysis of whey protein and functional properties[J]. Science and Technology of Food Industry, 2017, (04): 127-131. DOI: 10.13386/j.issn1002-0306.2017.04.016

限制性酶解乳清蛋白功能性质研究

Study on limited enzymatic hydrolysis of whey protein and functional properties

  • 摘要: 探究乳清蛋白在碱性蛋白酶限制性水解下功能性质变化。以乳清蛋白的溶解性,乳化性、乳化稳定性,起泡性、起泡稳定性为考察指标,确定乳清蛋白的等电点及分析不同水解度下乳清蛋白功能性质在p H调控下的变化。结果表明:乳清蛋白的等电点为4.8。乳清蛋白进行限制性酶解后功能性质有了很大提高,其中溶解性在DH14、p H10下达到最大值,较原蛋白提高了14.55%;起泡性在DH14、p H4下达到最大值,较原蛋白提高了107.5%;起泡稳定性在DH4、p H4下达到最大值,比原蛋白提高了8.66%;乳化性在DH14、p H12下达到最大值,比原蛋白提高了56.1%;乳化稳定性DH4、p H12下达到最大值,比原蛋白提高了50.42%。 

     

    Abstract: Explored the whey protein functional properties change under alkaline protease restrictive hydrolysis. Using whey protein solubility,emulsification and emulsion stability,foaming and foaming stability as indicators and determined the whey protein isoelectric point and analyzed different degree of hydrolysis of whey protein different functional properties under the p H.The results showed that whey protein isoelectric point was 4.8. Whey protein functional properties had greatly improved under limited enzymatic hydrolysis.Hydrolysis reached the maximum under DH14,p H10,higher than native protein 14.55%,foaming reached the maximum higher than native protein 107.5% under DH14,p H4,foaming stability reached the maximum under DH4,p H4 higher than native protein 8.66%; emulsifying reached the maximum under DH14,p H12 higher than native protein 56.1%,emulsion stability reached the maximum under DH4,p H12 higher than native protein 50.42%.

     

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