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首页> 外文期刊>日本食品科学工学会誌 >Extraction and enzymatic degradation of antimicrobial peptides, alpha andbeta-thionins, from barley and wheat [Japanese]
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Extraction and enzymatic degradation of antimicrobial peptides, alpha andbeta-thionins, from barley and wheat [Japanese]

机译:抗菌肽,α和小麦的抗菌肽,α和β-胞嘧啶的提取和酶促降解[日文]

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摘要

Antimicrobial peptides, alpha and beta-thionins, were extracted from barley and wheat flour wit 0.075- 0.15 N HCl. The degradation of alpha and beta-thionins by digestive enzymes at 37 degrees C was examined in vitro. No degradation of alpha-thionin was observed after the incubation of 10 mu g of barley alpha-thionin. Denaturated wheat alpha-thionin by S-pyridylethyl modification of cystine residues was degraded by pepsin. Trypsin (0.5 mu g) and chymotrypsin (5 mu g) degraded 9.1 mu g and 7.2 mu g of wheat alpha-thionin for 1 hr, and produced some partially hydrolyzed peptides. Similar results were obtained for barley alpha and beta-thionins. The partially hydrolyzed peptides had no more antibacterial activity. The partially hydrolyzed peptides were almost completely degraded by leucine aminopeptidase and carboxypeptidase A.
机译:抗微生物肽,α和β-胞嘧啶从大麦和小麦面粉提取0.075- 0.15n HCl中萃取。 体外检查37℃下消化酶的α和β-胞嘧啶的降解。 在孵育10μg大麦α-thionin之后,没有观察到α-thionin的降解。 通过S-吡啶基乙基改性胱氨酸残基改性的变性小麦α-硫酮蛋白酶降解。 胰蛋白酶(0.5μg)和胰凝乳蛋白酶(5μg)降解9.1μg和7.2μg小麦α-thionin 1小时,并产生一些部分水解的肽。 对于大麦α和β-胞胎蛋白获得了类似的结果。 部分水解的肽没有更多的抗菌活性。 部分水解的肽几乎完全通过亮氨酸氨基肽酶和羧肽酶A降解。

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