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中国精品科技期刊2020
黄赛博, 林慧敏, 邓尚贵. 响应面法优化带鱼蛋白多肽螯合亚铁制备工艺[J]. 食品工业科技, 2016, (04): 266-270. DOI: 10.13386/j.issn1002-0306.2016.04.045
引用本文: 黄赛博, 林慧敏, 邓尚贵. 响应面法优化带鱼蛋白多肽螯合亚铁制备工艺[J]. 食品工业科技, 2016, (04): 266-270. DOI: 10.13386/j.issn1002-0306.2016.04.045
HUANG Sai-bo, LIN Hui-min, DENG Shang-gui. Optimization of preparation conditions of hairtail protein polypeptide-Iron(Ⅱ) chelate by response surface methodology[J]. Science and Technology of Food Industry, 2016, (04): 266-270. DOI: 10.13386/j.issn1002-0306.2016.04.045
Citation: HUANG Sai-bo, LIN Hui-min, DENG Shang-gui. Optimization of preparation conditions of hairtail protein polypeptide-Iron(Ⅱ) chelate by response surface methodology[J]. Science and Technology of Food Industry, 2016, (04): 266-270. DOI: 10.13386/j.issn1002-0306.2016.04.045

响应面法优化带鱼蛋白多肽螯合亚铁制备工艺

Optimization of preparation conditions of hairtail protein polypeptide-Iron(Ⅱ) chelate by response surface methodology

  • 摘要: 以带鱼鱼糜为原料,研究带鱼蛋白多肽和亚铁离子的螯合工艺条件。分别以螯合反应p H、螯合温度、时间、Fe Cl2溶液与酶解液体积比、抗坏血酸添加量为主要研究对象,在单因素实验进行螯合率测定的基础上,通过Box-Behnken设计响应面优化实验。结果显示,螯合反应的最佳工艺参数为p H6.9,温度29℃,螯合时间30 min,Fe Cl2溶液与酶解液体积比为1∶50,抗坏血酸添加量为酶解液质量的0.1%,该条件下得到的螯合率为80.46%。红外图谱研究表明,螯合前后结构发生改变,证明带鱼蛋白多肽和亚铁离子确实形成新的螯合物。 

     

    Abstract: The preparation conditions of hairtail protein polypeptides chelating iron(Ⅱ) were studied,with hairtail surimi as raw materials. The influences of p H,temperature,time,solution volume ratio of Fe Cl_2 to enzymatic hydrolysate and ascorbic acid content on the yield of peptide- iron( Ⅱ) chelate were investigated. The optimization experiments of response surface were designed by Box-Behnken based on above one-factor experiments. The results showed that the optimal chelating conditions were p H6.9,29 ℃,30 min,Fe Cl_2-enzymatic hydrolysate volume ratio 1∶50(V/V),and ascorbic acid content 0.1% of hydrolysate. Under these conditions,the yield of peptide-iron(Ⅱ) chelate was 80.46%. The analysis of infrared spectrum revealed that the ferrous ions were chelated with the amino groups and carboxyl groups,which suggested the formation of a new kind of peptide-iron(Ⅱ) chelate.

     

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