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牡蛎抗氧化活性肽的酶解工艺研究
引用本文:汪秋宽,宋琳琳,徐玲,刘红丹,何云海,任丹丹,虞星炬.牡蛎抗氧化活性肽的酶解工艺研究[J].大连水产学院学报,2009,24(2):95-99.
作者姓名:汪秋宽  宋琳琳  徐玲  刘红丹  何云海  任丹丹  虞星炬
作者单位:1. 中国科学院,大连物理化学研究所,辽宁,大连,116023;大连水产学院,辽宁省水产品加工及综合利用重点开放实验室,辽宁,大连,116023
2. 大连水产学院,辽宁省水产品加工及综合利用重点开放实验室,辽宁,大连,116023
3. 中国科学院,大连物理化学研究所,辽宁,大连,116023
摘    要:以木瓜蛋白酶和中性蛋白酶为工具酶,利用正交试验法确定了木瓜蛋白酶和中性蛋白酶酶解制备牡蛎抗氧化活性肽的最佳酶解工艺。结果表明:当时间为150min、酶用量为6%、温度为45℃、pH为7.0时,木瓜蛋白酶酶解液的抗氧化活性最强;当时间为110min、酶用量为3%、温度为65℃、pH为6.0时,中性蛋白酶酶解液的抗氧化活性最强。用SephadexG-15葡聚糖凝胶柱层析分析的结果表明,木瓜蛋白酶酶解液中最佳抗氧化活性组分的相对分子质量为1191和826左右,中性蛋白酶酶解液最佳抗氧化活性组分的相对分子质量为1074和735左右,其抗氧化活性峰值与蛋白肽在280nm下的吸收峰值分别相吻合。

关 键 词:牡蛎  酶解工艺  抗氧化活性肽

The hydrolyzing technologies of oysterCrassostrea gigas antioxidation peptides
WANG Qiu-kuan,SONG Lin-lin,XU Ling,LIU Hong-dan,HE Yun-hai,REN Dan-dan,YU Xing-ju.The hydrolyzing technologies of oysterCrassostrea gigas antioxidation peptides[J].Journal of Dalian Fisheries University,2009,24(2):95-99.
Authors:WANG Qiu-kuan  SONG Lin-lin  XU Ling  LIU Hong-dan  HE Yun-hai  REN Dan-dan  YU Xing-ju
Institution:WANG Qiu-kuan1,2,SONG Lin-lin2,XU Ling2,LIU Hong-dan2,HE Yun-hai2,REN Dan-dan2,YU Xing-ju1 (1.Biotechnology Division,Dalian Chemical , Physics Institute,Chinese Academy of Science,Dalian 116023,China,2.The Key , Open Laboratory of Fishery Product Processing , Utilization of Liaoning Province,Dalian Fisheries Univ.,China)
Abstract:The hydrolysis process and antioxidation measured in scavenging activities of hydroxyl radicals in the hydrolysates were optimized for peptides of Pacific oyster Crassostrea gigas by papain and neutral protease in orthogohal experiments. The maximal activity of scavenging hydroxyl radicals was found in the papain hydrolysate under the follow conditions of hydrolytic period of 150 min, 6% of the enzyme supplementation, at 45 ℃ and pH 7.0. The maximal activity of scavenging hydroxyl radicals was observed in the neutral protease hydrolysate under the follow conditions of hydrolytic period of 110 min, 3% of the enzyme supplementation, at 65 ℃ and pH 6.0. The sephadex G - 15 analysis revealed that there were considerable variations in the scavenging hydroxyl radical activity of different peptide fractions. The peptide hydrolyzed by the papain had molecular weight of about 1191 Dalton and 826 Dalton, with the maximal hydroxyl radical scavenging activity, while the peptide hydrolyzed by the neutral protease had molecular weight of about 1074 Dalton and 735 Dalton, with the maximal hydroxyl radical scavenging activity.
Keywords:oyster  enzyme hydrolytic technology  antioxidant peptide  
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