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机构地区:[1]西北农林科技大学食品科学与工程学院,陕西杨凌712100
出 处:《中国食品学报》2015年第5期90-95,共6页Journal of Chinese Institute Of Food Science and Technology
基 金:陕西省陕南突破发展基金项目〔2006ZKC(二)04-34〕;林业公益性行业科研专项经费子课题【国科发农字(201004027-04)】
摘 要:为优化碱性蛋白酶酶解魔芋飞粉蛋白制备抗氧化多肽的条件,采用响应面分析法,以·OH清除率为响应值,研究酶解温度、酶用量、酶解p H值对制备抗氧化肽的影响。此外,还研究了不同分子质量魔芋多肽的抗氧化活性,结果表明:最佳酶解工艺参数:底物质量分数2.25%、温度55℃、酶用量3 228 U/g底物、p H 7.84、水解时间270 min。该条件下抗氧化多肽(18.35 mg/m L)的·OH清除率为73.41%,多肽得率为75.37%。通过Sephadex G-25和Sephadex G-15串联柱分离得到5个多肽组分,其中分子质量为1 500 u和1 000 u的组分抗氧化活性较高,其清除DPPH·的IC50分别为2.82 mg/m L和3.65 mg/m L;清除·OH的IC50分别为9.03mg/m L和14.16 mg/m L;抑制大鼠肝脏自发性脂质过氧化的IC50分别为0.21 mg/m L和0.66 mg/m L;抑制大鼠红细胞H2O2诱导氧化溶血的IC50分别为0.11 mg/m L和0.22 mg/m L。In order to optimize enzymolysis technology for production of antioxidant peptides from Konjac fly powder protein, effect of enzyme concentration, enzymolysis temperature, and pH value on the technology in which the scaveng- ing rate to .OH was taken as response value was analyzed with response surface methodology. In addition, the antioxi- dant activities of polypeptide components with different molecular weight were studied. The results showed that the opti mum conditions were as follows: substrate concentration 2.25%, enzymolysis temperature 55 ℃, enzyme concentration 3 228 U/g, pH value 7.84, enzymolysis time 270min. Under such conditions, the scavenging rate to -OH of the antioxi- dant peptides (18.35 mg/mL) was 73.41%, rate of peptides production was 75.37%. Konjak peptides separated by Series Connection of Sephadex G-25 and Sephadex G-15 obtained two high antioxidant ability components with molecular weight l 500u and 1 000u, their DPPH- scavenging activity' ICso were 2.82mg/mL and 3.65 mg/mL; .OH scavenging activity' ICso were 9.03 mg/mL and 14.16 mg/mL; the inhibition ability of pontaneous lipid peroxidation' ICso were 0.21 mg/mL and 0.66mg/mL; the inhibition ability of erythrocyte hemolysis induced by H2Oz IC5o were 0.11 mg/mL and 0.22 mg/mL.
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