Production of Novel Polygalacturonase from Bacillus paralicheniformis CBS32 and Application to Depolymerization of Ramie Fiber
Production of Novel Polygalacturonase from Bacillus paralicheniformis CBS32 and Application to Depolymerization of Ramie Fiber
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DOI：
10.3390/polym11091525
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发表时间：
2019-09
期刊：
影响因子：
5
通讯作者：
M. Rahman;Y. Choi;Young Kyun Kim;Chulhwan Park;J. Yoo
中科院分区：
文献类型：
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作者：
M. Rahman;Y. Choi;Young Kyun Kim;Chulhwan Park;J. Yoo
多聚半乳糖醛酸酶（EC. 3.2.1.15）是水解半乳糖醛酸之间的α-1，4糖苷键的酶。本研究从韩国泡菜中分离出一株产碱性多聚半乳糖醛酸酶的地衣芽孢杆菌CBS 32。16 SrRNA序列分析表明，该菌株与B菌株的同源性为99.92%，与B菌株的同源性为99.92%。地衣芽孢杆菌KJ 16 LBMN 01000156.来自B的多聚半乳糖醛酸酶。纯化的PN 32产率为16.8%，纯度为粗发酵液的33倍。通过SDS-PAGE测定分子量为110 kDa，并通过酶谱分析确认活性条带。PN 32的N端氨基酸序列为Gly-Val-Lys-Glu-Val-X-Gln-Thr-Phe。在序列比较中，PN 32被认为是一种新的多聚半乳糖醛酸酶，因为该序列与以前的报道不匹配。将PN 32酶解苎麻纤维进行脱胶试验，结果表明，PN 32酶解苎麻纤维的能力比市售果胶酶高28%。总的来说，根据结果，PN 32具有很高的工业应用潜力。
Polygalacturonase (EC. 3.2.1.15) is an enzyme that hydrolyzes the alpha-1,4 glycosidic bonds between galacturonic acid. In this study, an alkaline polygalacturonase producer Bacillus paralicheniformis CBS32 was isolated from kimchi (conventional Korean fermented food). The 16S rRNA sequence analysis of the isolated strain revealed that it was 99.92% identical to B. paralicheniformis KJ 16LBMN01000156. The polygalacturonase from B. paralicheniformis CBS32 was named PN32, and the purified PN32 showed a 16.8% yield and a 33-fold purity compared to the crude broth. The molecular mass, 110 kDa, was determined by SDS-PAGE, and the active band was confirmed by zymography analysis. The N-terminal amino acid sequence residues of PN32 were determined to be Gly–Val–Lys–Glu–Val–X–Gln–Thr–Phe. In the sequence comparison, PN32 was suggested as a novel polygalacturonase, since the sequence was not matched with the previous reports. In an application study, enzymatic depolymerization of ramie was performed for fiber degumming, and the result showed that the PN32 had a 28% higher depolymerization compared to the commercial pectinase. Overall, based on the results, PN32 has high potential for industrial applications.