Unlocking bioinformatics and structural insights of a novel thermo-alkaline pectate lyase ScpB from Phytophthora parasitica INRA-310

IF 5.9 1区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

Food Bioscience Pub Date : 2025-09-25 DOI:10.1016/j.fbio.2025.107662

Mei Zhao , Xiaohong Pan , Jiaojiao Chen , Jie Shang , Yiwei Zhang , Cunsheng Zhang , Liang Guo , Xianghui Qi

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Abstract

Pectate lyase (PEL) has broad industrial utility, but its application is limited by insufficient thermal stability and alkali tolerance. In this study, a novel PEL (hereafter, ScpB) from Phytophthora parasitica INRA-310 was identified for the first time through data-driven mining and bioinformatics. Homology modeling revealed that ScpB consists of two domains: a PEL superfamily-associated domain ScpB-I and a catalytic domain ScpB-II, which are connected by a short linker region. Based on truncated engineering and protein structure engineering strategies, ScpB-I and ScpB-II must cooperate to exhibit the PEL activity. Furthermore, ScpB was recruited for developing biochemical properties. The purified ScpB exhibited optimal activity at pH 10.0 and 55 °C, aligning with textile biorefining conditions. Notably, in the presence of Ca²⁺ and Fe³⁺, a 215.97 % and 182.08 %, respectively, improvement in catalytic activity compared to the control group without metal ion. Finally, the bioscouring assay was carried out, ScpB exhibited a significant increase in the wetted fabric area to 5.371 ± 0.382 cm², which was 3.6 times that of the untreated sample (1.496 cm²). Scanning electron microscopy confirmed effective pectin removal and smoother fibers. This study expands the PEL resource library and offers a promising enzyme for efficient, eco-friendly textile biorefining.

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从疫霉INRA-310中提取的新型热碱性果胶裂解酶ScpB的生物信息学和结构分析

果胶裂解酶（PEL）具有广泛的工业用途，但其热稳定性和耐碱性不足，限制了其应用。本研究利用数据驱动挖掘和生物信息学技术，首次从疫霉菌INRA-310中鉴定出一个新的PEL（以下简称ScpB）。同源性建模显示，ScpB由两个结构域组成：PEL超家族相关结构域ScpB- i和催化结构域ScpB- ii，它们通过短连接子区域连接。基于截断工程和蛋白结构工程策略，ScpB-I和ScpB-II必须协同发挥PEL活性。此外，ScpB被用于发展生化特性。纯化后的ScpB在pH 10.0和55℃条件下具有最佳活性，符合纺织生物精制条件。值得注意的是，在Ca2+和Fe3+的存在下，催化活性分别比不含金属离子的对照组提高了215.97%和182.08%。最后进行生物洗涤试验，ScpB在织物上的浸湿面积显著增加，达到5.371±0.382 cm2，是未处理样品（1.496 cm2）的3.6倍。扫描电子显微镜证实有效的果胶去除和更光滑的纤维。这项研究扩大了PEL资源库，并为高效、环保的纺织品生物精制提供了一种有前途的酶。

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来源期刊

Food Bioscience Biochemistry, Genetics and Molecular Biology-Biochemistry

CiteScore

6.40

自引率

5.80%

发文量

671

审稿时长

27 days

期刊介绍： Food Bioscience is a peer-reviewed journal that aims to provide a forum for recent developments in the field of bio-related food research. The journal focuses on both fundamental and applied research worldwide, with special attention to ethnic and cultural aspects of food bioresearch.