| 姜太玲,吴红洋,董小华，等.花椒籽蛋白抗菌肽的分离纯化研究[J].中国油脂,2015,40(10):.[JIANG Tailing,WU Hongyang,DONG Xiaohua，etc.Isolation and purification of antimicrobial peptides from prickly ash （Zanthoxylum bungeanum Maxim） seed protein[J].China Oils and Fats,2015,40(10):.] |
| 花椒籽蛋白抗菌肽的分离纯化研究 |
| Isolation and purification of antimicrobial peptides from prickly ash （Zanthoxylum bungeanum Maxim） seed protein |
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| DOI： |
| 中文关键词: 花椒籽蛋白 抗菌肽 抑菌率 分离纯化 相对分子质量 |
| 英文关键词:prickly ash seed protein antimicrobial peptide inhibitory rate isolation and purification relative molecular weight |
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| 中文摘要: |
| 分别用胃蛋白酶、酸性蛋白酶酶解花椒籽蛋白制得两种粗酶液（A肽和B肽），以抑菌率为指标，依次采用超滤、Sephadex G-50凝胶层析进行分子截留和分离纯化，用Tricine-SDS-PAGE电泳测定其主要抗菌肽的相对分子质量。结果显示：两种酶解产物的粗酶液经超滤后，获得的相对分子质量为5~10 kD的组分（A-b肽和B-b肽）对大肠杆菌的抑菌率最高，分别为62.79%和66.94%；将A-b肽和B-b肽进行凝胶层析，分别分离得4个组分，其中A-b肽活性最大的是组分G4（A-b-Ⅳ肽），对大肠杆菌的抑菌率为100%，B-b肽活性最大的是组分F3（B-b-Ⅲ肽），对大肠杆菌的抑菌率为6999%；A-b-Ⅳ肽和B-b-Ⅲ肽的相对分子质量分别为8.11 kD和10.80 kD。 |
| 英文摘要: |
| Prickly ash (Zanthoxylum bungeanum Maxim) seed protein was hydrolyzed with pepsin and acid protease respectively. With inhibitory rate as indicator, the crude enzyme solutions (peptide A and peptide B) were in turn molecular retained, isolated and purified by ultrafiltration and Sephadex G-50 gel chromatography. The relative molecular weights of the main antimicrobial peptides were measured by Tricine-SDS-PAGE. The results showed that after the crude enzyme solutions of two hydrolysates were ultrafiltrated, the components with the relative molecular weights in the range of 5-10 kD (peptide A-b and peptide B-b) had the highest antibacterial activity on E.coli
, reaching 62.79% and 66.94%. Four components were isolated from peptide A-b and peptide B-b by gel chromatography. Components G4 (peptide A-b-Ⅳ) from peptide A-b had the highest antibacterial activity, and the inhibitory rate on E.coli was 100%. Components F3 (peptide B-b-Ⅲ) from peptide B-b had the highest antibacterial activity, and the inhibitory rate on E.coli was 69.99%.The relative molecular weights of peptide A-b-Ⅳ and peptide B-b-Ⅲ were 8.11 kD and 10.80 kD, respectively. |
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