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作 者:郭晨晨 耿宏庆 徐毅[1] 唐永欣 尚永彪[1,2] GUO Chenchen;GENG Hongqing;XU Yi;TANG Yongxin;SHANG Yongbiao(College of Food Science,Southwest University,Chongqing 400715,China;Chongqing Key Laboratory of Specialty Foods Jointly Built by Sichuan and Chongqing,Chongqing 400715,China)
机构地区:[1]西南大学食品科学学院,重庆400715 [2]川渝共建特色食品重庆市重点实验室,重庆400715
出 处:《食品与发酵工业》2024年第12期202-208,共7页Food and Fermentation Industries
基 金:重庆市技术创新与应用发展专项(cstc2020jscx-tpyzxX0011)。
摘 要:猪肝是优质的动物蛋白来源,但天然猪肝蛋白乳化性较差,为了改善其性质,提升猪肝的加工附加值,该实验制备猪肝蛋白溶液,以琥珀酸酐的添加量为变量,测定酰化度指标并考察对猪肝蛋白乳化性质、蛋白质颗粒状态、分子结构等的影响。结果表明,随着琥珀酸酐添加量的增加,猪肝蛋白的酰化度、乳化活性总体呈上升趋势,乳液Zeta电位以及乳液油滴表面蛋白质吸附量呈先升高后下降的趋势,乳液粒径、蛋白质表面疏水性呈下降趋势,蛋白质的高级结构发生了变化。猪肝蛋白溶液(质量浓度10 mg/mL)酰化处理时琥珀酸酐的最佳添加量为0.10 g/g Pro,此条件下猪肝蛋白的乳化活性由9.550 m^(2)/g提高到了64.135 m^(2)/g。琥珀酸酐通过共价结合与猪肝蛋白发生反应,引起蛋白质结构的改变,能显著改善猪肝蛋白的乳化活性。Pig liver is a high-quality source of animal protein,but natural pig liver protein is poorly emulsified.To improve its properties and enhance the added value of pig liver processing,this experiment prepared pig liver protein solution,measured the index of acylation,and investigated the effects on the emulsification properties,protein particle state,and molecular structure of pig liver protein with the addition amount of succinic anhydride as the variable.Results showed that with the increase of succinic anhydride addition,the acylation degree and emulsification activity of porcine liver protein showed an overall increasing trend,the emulsion zeta potential and the protein adsorption on the surface of emulsion oil droplets showed an increasing trend and then a decreasing trend,the emulsion particle size and protein surface hydrophobicity showed a decreasing trend,and the advanced structure of the protein were changed.The optimal addition of succinic anhydride for acylation treatment of porcine liver protein solution(10 mg/mL of concentration)was 0.10 g/g Pro.The emulsification activity of the porcine liver protein increased from 9.550 m^(2)/g to 64.135 m^(2)/g under this condition.Succinic anhydride reacted with porcine liver protein through covalent binding,causing changes in protein structure and significantly improving the emulsifying activity of the porcine liver protein.
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