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抗菌肽Leg1在溶液及肉类中的稳定性与活性及其从鹰嘴豆储存蛋白的优化生成

Stability and Activity of the Antimicrobial Peptide Leg1 in Solution and on Meat and Its Optimized Generation from Chickpea Storage Protein.

作者信息

Heymich Marie-Louise, Srirangan Showmika, Pischetsrieder Monika

机构信息

Chair of Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Str. 10, 91058 Erlangen, Germany.

出版信息

Foods. 2021 May 25;10(6):1192. doi: 10.3390/foods10061192.

DOI:10.3390/foods10061192
PMID:34070446
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8227015/
Abstract

The antimicrobial peptide Leg1 (RIKTVTSFDLPALRFLKL) from chickpea legumin is active against spoilage bacteria, yeast, and mold. The present study tested its effectiveness under food storage conditions and examined options to obtain a food-grade agent. The minimum inhibitory concentration (MIC) of Leg1 against   (62.5 µM) proved stable over seven days at 20 °C or 4 °C. It was not influenced by reduced pH (5.0 vs. 6.8), which is relevant in food such as meat. An incubation temperature of 20 °C vs. 37 °C reduced the MIC to 15.6/7.8 µM against  / . With a minimum bactericidal concentration in meat of 125/15.6 µM against   , Leg1 is equivalently effective as nisin and 5000-82,000 times more active than sodium benzoate, potassium sorbate, or sodium nitrite. Replacing the counter-ion trifluoroacetate derived from peptide synthesis by the more natural alternatives acetate or chloride did not impair the activity of Leg1. As an alternative to chemical synthesis, an optimized protocol for chymotryptic hydrolysis was developed, increasing the yield from chickpea legumin by a factor of 30 compared to the standard procedure. The present results indicate that food-grade Leg1 could possibly be applicable for food preservation.

摘要

来自鹰嘴豆球蛋白的抗菌肽Leg1(RIKTVTSFDLPALRFLKL)对腐败细菌、酵母和霉菌具有活性。本研究测试了其在食品储存条件下的有效性,并研究了获得食品级制剂的方法。Leg1对(62.5 µM)的最低抑菌浓度(MIC)在20°C或4°C下7天内保持稳定。它不受pH降低(5.0对6.8)的影响,这在肉类等食品中是相关的。20°C与37°C的孵育温度使针对/的MIC降至15.6/7.8 µM。Leg1在肉类中的最低杀菌浓度为125/15.6 µM,与乳酸链球菌素等效,且比苯甲酸钠、山梨酸钾或亚硝酸钠活性高5000 - 82000倍。用更天然的替代物乙酸盐或氯化物取代肽合成中衍生的抗衡离子三氟乙酸盐不会损害Leg1的活性。作为化学合成的替代方法,开发了一种用于胰凝乳蛋白酶水解的优化方案,与标准程序相比,鹰嘴豆球蛋白的产量提高了30倍。目前的结果表明,食品级Leg1可能适用于食品保鲜。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8ad/8227015/15938da098c8/foods-10-01192-g002a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8ad/8227015/20ac01f460e7/foods-10-01192-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8ad/8227015/15938da098c8/foods-10-01192-g002a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8ad/8227015/20ac01f460e7/foods-10-01192-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c8ad/8227015/15938da098c8/foods-10-01192-g002a.jpg

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