从土壤分离株层出镰刀菌 NFCCI 1769 中生产和纯化外聚半乳糖醛酸酶及其应用。
Production, Purification of Exo-Polygalacturonase from Soil Isolate Paecilomyces variotii NFCCI 1769 and Its Application.
机构信息
Department of Microbiology, SSVPS's Lk. Dr. P. R. Ghogrey Science College, Dhule, 424005 Maharashtra India.
出版信息
Indian J Microbiol. 2012 Jun;52(2):240-6. doi: 10.1007/s12088-011-0162-x. Epub 2011 Feb 14.
The aim of the present study was to produce exo-polygalacturonase from potent soil isolate by submerged fermentation and its application for fruit juice treatment. Pectinase producing strains were selectively isolated from pectin industry waste. A selected isolate C2 was found to produce significant amount of exo-polygalacturonase. The isolate was identified as Paecilomyces variotii on the basis of morphological characteristics and 18S rRNA gene sequence analysis. The exo-polygalacturonase produced by the isolate was purified by ammonium sulphate precipitation, size exclusion chromatography and ion exchange chromatography. The purified enzyme had MW of 39.4 kD based on SDS PAGE. Under partially optimized conditions, purified exo-polygalacturonase showed specific activity of 98.49 U/mg protein at pH 6.0 and 30°C. The enzyme was comparatively stable from 10 to 30°C and the activity decreased with increasing temperature. Purified enzyme brought about considerable reduction in viscosity of fruit juice samples.
本研究旨在通过深层发酵从有潜力的土壤分离株中生产外聚半乳糖醛酸酶，并将其应用于果汁处理。从果胶工业废物中选择性地分离出产果胶酶的菌株。发现一株分离株 C2 能大量产生外聚半乳糖醛酸酶。根据形态特征和 18S rRNA 基因序列分析，该分离株被鉴定为多形拟青霉。用硫酸铵沉淀、分子筛层析和离子交换层析对分离株产生的外聚半乳糖醛酸酶进行了纯化。根据 SDS-PAGE，纯化酶的 MW 为 39.4 kD。在部分优化条件下，纯化的外聚半乳糖醛酸酶在 pH 6.0 和 30°C 时表现出 98.49 U/mg 蛋白的比活性。该酶在 10 至 30°C 之间相对稳定，活性随温度升高而降低。纯化酶使果汁样品的粘度显著降低。
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