A new alkaline pectin lyase with novel thermal and pH stability from Bacilus velezensis

IF 1.4 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Protein expression and purification Pub Date : 2024-08-05 DOI:10.1016/j.pep.2024.106564

Ze Li, Su-Yan Tian

引用次数: 0

Abstract

Pectin lyases are important in various industries, including tobacco leaves processing. In this paper, a novel pectin lyase Pel04 from Bacillus velezensis was characterized. Pel04 molecular weight (Mw) and isoelectric point (pI) of the protein sequence after removing the signal peptide are 43.0 kDa. The optimal temperature and pH of Pel04 is 50 °C and 9.0, respectively. Pel04 was stable in the range of 30–50 °C, and pH 9.5–11. Ca²⁺ can significantly stimulate the enzyme activity, while Cu²⁺, Co²⁺, Fe³⁺, and Mn²⁺ have inhibitory effects on Pel04. By Pel04 treatment, the overall content of acids, alcohols, esters and other aromas in tobacco leaves increased, while the contents of phenolic and heterocyclic substances decreased. Pel04 has important potential for industrial application particularly in improving quality of tobacco leaves.

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来自 Velezensis 杆菌的一种具有新型热稳定性和 pH 稳定性的新型碱性果胶裂解酶。

果胶裂解酶在包括烟叶加工在内的各行各业中都很重要。本文鉴定了一种新型果胶裂解酶 Pel04。除去信号肽后，Pel04 蛋白序列的分子量（Mw）和等电点（pI）均为 43.0 kDa。Pel04 的最适温度和 pH 值分别为 50 °C 和 9.0。Pel04 在 30-50 °C 和 pH 9.5-11 范围内稳定。Ca2+ 能明显刺激酶的活性，而 Cu2+、Co2+、Fe3+ 和 Mn2+ 则对 Pel04 有抑制作用。经 Pel04 处理后，烟叶中酸、醇、酯等香气物质的总含量增加，而酚类和杂环类物质的含量减少。Pel04 具有重要的工业应用潜力，特别是在提高烟叶质量方面。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Protein expression and purification 生物-生化研究方法

CiteScore

3.70

自引率

6.20%

发文量

120

审稿时长

32 days

期刊介绍： Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.