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作 者:陈悦[1] 李琦[1] 佟长青[1] 曲敏[1] 李伟[1]
机构地区:[1]大连海洋大学食品科学与工程学院,辽宁大连116023
出 处:《河北渔业》2015年第10期9-12,共4页
基 金:辽宁省教育厅科学研究项目(L2013277);海洋局公益性行业科研专项(项目编号201205022-7)
摘 要:采用胰蛋白酶对魁蚶蛋白进行不同时间的酶解,比较酶解产物的抑菌活性。选取抑菌活性较好的胰蛋白酶酶解产物进行细菌呼吸抑制研究。通过RP-HPLC对该酶解产物进行分离纯化,采用质谱分析其氨基酸序列。结果表明,胰蛋白酶酶解0.5h所得到的酶解产物对金黄色葡萄球菌及希瓦氏菌具有较好的抑菌活性。其抑制金黄色葡萄球菌和希瓦氏菌的HMP途径。RP-HPLC分离纯化得到了4个抑菌活性较好的组分。对其中第2组分进行质谱分析得到3个目标多肽,其m/z分别为679、792及905,将这3个目标多肽导入De novo Explorer(TM)Software(AB SCIEX;Version 4.1)进行分析,获得了候选抑菌肽氨基酸序列。Scapharca Broughtonii proteins were digested using trypsin for different time,and the antibacterial activities of the obtained hydrolysates were investigated.Inhibition of respiration was carried out using the hydrolysates with stronger antibacterial activities.The hydrolysates were isolated and purified on RP-HPLC column,and the amino acid sequences were analyzed by mass spectrometry.The results showed that the hydrolysates digested by typsin for 0.5hcould better inhibit the growth of Staphylococcus aureus and Shewanellasp.They inhibited Hexose Monophophate Pathway(HMP)of S.aureus and Shewanellasp.Four fractions with better antibacterial activities were isolated and purified on RP-HPLC column.Three peptides found in the 2nd fraction were analyzed by MS/MS,and their m/z were 679,792 and 905,respectively.The three peptides were analyzed using De novo Explorer(TM)Software(AB SCIEX;Version 4.1)and the candidate amino acid sequences were obtained.
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