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首页> 外文期刊>International Dairy Journal >Antibacterial activity of bovine milk lactoferrin and its hydrolysates prepared with pepsin, chymosin and microbial rennet against foodborne pathogen Listeria monocytogenes
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Antibacterial activity of bovine milk lactoferrin and its hydrolysates prepared with pepsin, chymosin and microbial rennet against foodborne pathogen Listeria monocytogenes

机译:胃蛋白酶,凝乳酶和微生物凝乳酶制备的牛乳乳铁蛋白及其水解产物对食源性单核细胞增生李斯特菌的抗菌活性

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摘要

Lactoferrin is an iron binding glycoprotein that contains antimicrobial peptides in its structure, which are released when hydrolysed by proteases. The antibacterial activity of bovine lactoferrin, its hydrolysates obtained with pepsin, chymosin and microbial rennet, and bovine whey fractions, has been assayed against Listeria monocytogenes serovar 4b in this study. The hydrolysates obtained with each enzyme were found to be inhibitory of bacterial growth; although the activity was lower than that exerted by the whole lactoferrin, except at low concentrations for chymosin and microbial rennet hydrolysates. The antibacterial activity of all the hydrolysates corresponded to the fraction with a molecular mass higher than 3 kDa. The peptides of hydrolysates were fractionated by using sulfonic acid derivatives and the cationic peptides analysed by matrix-assisted laser desorption ionisation-time of flight mass spectrometry. Moreover, some antibacterial activity was found in fractions obtained from bovine whey by size exclusion chromatography. (C) 2015 Elsevier Ltd. All rights reserved.
机译:乳铁蛋白是一种铁结合糖蛋白,其结构中含有抗菌肽,当被蛋白酶水解时会释放出抗菌肽。在这项研究中,已经测定了牛乳铁蛋白,通过胃蛋白酶,凝乳酶和微生物凝乳酶获得的水解产物以及牛乳清级分的抗细菌活性。发现用每种酶获得的水解产物均能抑制细菌的生长。尽管活性低于全乳铁蛋白,但凝乳酶和微生物凝乳酶水解产物的浓度低。所有水解产物的抗菌活性对应于分子量高于3kDa的级分。通过使用磺酸衍生物对水解产物的肽进行分级分离,并通过基质辅助激光解吸电离飞行时间质谱分析阳离子肽。此外,在通过大小排阻色谱法从牛乳清获得的级分中发现了一些抗菌活性。 (C)2015 Elsevier Ltd.保留所有权利。

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