基于带鱼(Trichiurus lepturus)蛋白复合酶解液中ABP对G–等微生物的致死结构及表征活性分析

ANTIBACTERIAL ACTIVITY OF HAIRTAIL(TRICHIURUS LEPTURUS) PROTEIN PEPTIDE AND THE FOOD PHYSICOCHEMICAL PROPERTIES

为研究带鱼(Trichiurus lepturus)蛋白复合酶解液中抗菌肽(ABP)的抑菌性及表征活性,本文以舟山小带鱼为研究对象,制备蛋白抗菌肽。研究得到抗菌肽分子量在区间(>3000Da,3000-800Da,<800Da)内均有分布,在3000-800Da区间内含量达到49.61%,酶解程度最深,氨基酸总量为881.83mg/g,必需氨基酸与氨基酸总量比为44.75%,必需氨基酸与非必需氨基酸比为81.33%,营养价值高。六类提升抗菌效力的氨基酸占氨基酸总量42.71%,抗菌效力较高,具有广谱抗菌活性,为阳离子型抗菌肽,对G–具有较强的抑菌效能。抗菌效力与稀释128倍(10.15U/mL)土霉素抗菌效力相当,与稀释4倍的硫酸链霉素(325U/mL)抗菌效力相当。对抗菌肽的表征活性进行研究表明:该抗菌肽在pH 2-12下溶解度良好,均大于88%,有强适应性;乳化性随pH增大而增强,pH 4时乳化性最低,为53.68%,在pH 12时达到最高值78.34%;乳化稳定性在pH 6时达到最高,为85.83%,pH环境过酸或者过碱的情况下乳化稳定性均较低;发泡性随pH上升呈现增长趋势,在pH 12时达到最大值57.33%,pH 4时抗菌肽泡沫稳定性最低,为22.86%,pH升高,泡沫稳定性也随之增强,在pH 12时达到最大值59.58%。该研究结果对探究带鱼抗菌肽的各项性质提供了理论依据,对带鱼抗菌肽的应用研究具有一定的理论指导意义。

To study the antibacterial activity and food physicochemical properties of fish protein antibacterial peptide,we took hairtail Trichiurus lepturus as the research object for the preparation of protein antimicrobial peptide.The molecular weight of the antimicrobial peptides was distributed in the ranges of>3000,3000-800,and<800 Da.The content reached 49.61%in the range of 3000-800 Da at which enzymatic hydrolysis was the deepest.The total amount of amino acids was 881.83 mg/g;the ratio of essential amino acids to amino acids was 44.75%;the ratio of essential amino acids to non-essential amino acids is 81.33%;and the nutritional value is high.Six types of amino acids enhanced the antibacterial efficacy and they accounted for 42.71%of the total amino acids,showing a high and broad-spectrum antibacterial activity and being a cationic antibacterial peptide.The antibacterial efficacy is equal to that of 128-fold(10.15 U/mL)diluted oxytetracycline,and that of the 4-fold dilution of streptomycin sulfate(325 U/mL).The antimicrobial peptide had a good solubility at pH 2-12,reaching 88%,and has strong adaptability.Emulsification increased with increasing pH from the lowest emulsifiability of 53.68%at pH 4 to the highest of 78.34%at pH 12.The emulsification stability reached the highest of 85.83%at pH 6,and was low in the two ends of pH scale.The foaming property increased with the increase of pH value,reaching the maximum of 57.33%at pH 12.The antibacterial peptide foam had the lowest stability at pH 4 for 22.86%only,and peaked to 59.58%at pH 12.The results of this study provide a theoretical basis for exploring properties and applications of the antibacterial peptides.