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[乳酸乳球菌乳酸亚种Al2中乳链菌肽的纯化及某些性质研究]

[Studies on purification and some properties of nisin from Lactococcus lactis subsp. lactis Al2].

作者信息

Chen X, He S, Long L, Huan L, Xue Y

机构信息

Institute of Microbiology, Academia Sinica, Beijing.

出版信息

Wei Sheng Wu Xue Bao. 1996 Aug;36(4):269-75.

PMID:9639829
Abstract

Nisin from Lactococcus lactis subsp. lactis AL2 was extracted with n-propanol from NaCl-saturated culture and purified by ion-exchange chromotography on CM-Sephadex C-25. Nisin was purified 1.63 fold with a yield of 41.7%. The molecular weight of nisin was determined by SDS-PAGE to be about 3500. Nisin activity was stable at low pH and sensitive to digestion by a-chymotrypsin. Nisin is capable of inhibiting a broad range of gram-positive bacteria. In contrast, the gram-negative bacteria, yeasts, molds and Nip+ L. lactis subsp. lactis ATCC11454 were not inhibited.

摘要

从乳酸乳球菌乳酸亚种AL2中提取的乳链菌肽,用正丙醇从饱和氯化钠培养物中提取,并通过CM-葡聚糖凝胶C-25离子交换色谱法纯化。乳链菌肽纯化了1.63倍,产率为41.7%。通过SDS-PAGE测定乳链菌肽的分子量约为3500。乳链菌肽活性在低pH值下稳定,对α-胰凝乳蛋白酶消化敏感。乳链菌肽能够抑制多种革兰氏阳性菌。相比之下,革兰氏阴性菌、酵母、霉菌和乳酸乳球菌乳酸亚种ATCC11454未受到抑制。

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