دورية أكاديمية

Modification and application of highly active alkaline pectin lyase

التفاصيل البيبلوغرافية
العنوان: Modification and application of highly active alkaline pectin lyase
المؤلفون: Pi-Wu Li, Jun Ma, Xiao-Feng Wei, Zi-Yang Zhang, Rui-Ming Wang, Jing Xiao, Jun-Qing Wang
المصدر: AMB Express, Vol 12, Iss 1, Pp 1-10 (2022)
بيانات النشر: SpringerOpen, 2022.
سنة النشر: 2022
المجموعة: LCC:Biotechnology
LCC:Microbiology
مصطلحات موضوعية: Alkaline pectin lyase, Fragment replacement, Enzymatic activity, Molecular dynamics simulation, Biotechnology, TP248.13-248.65, Microbiology, QR1-502
الوصف: Abstract Alkaline pectate lyase has developmental prospects in the textile, pulp, paper, and food industries. In this study, we selected BacPelA, the pectin lyase with the highest expression activity from Bacillus clausii, modified and expressed in Escherichia coli BL21(DE3). Through fragment replacement, the catalytic activity of the enzyme was significantly improved. The optimum pH and temperature of the modified pectin lyase (PGLA-rep4) were 11.0 and 70 °C, respectively. It also exhibited a superior ability to cleave methylated pectin. The enzyme activity of PGLA-rep4, measured at 235 nm with 0.2% apple pectin as the substrate, was 554.0 U/mL, and the specific enzyme activity after purification using a nickel column was 822.9 U/mg. After approximately 20 ns of molecular dynamics simulation, the structure of the pectin lyase PGLA-rep4 tended to be stable. The root mean square fluctuation (RMSF) values at the key catalytically active site, LYS168, were higher than those of the wildtype PGLA. In addition, PGLA-rep4 was relatively stable in the presence of metal ions. PGLA-rep4 has good enzymatic properties and activities and maintains a high pH and temperature. This study provides a successful strategy for enhancing the catalytic activity of PGLA-rep4, making it the ultimate candidate for degumming and various uses in the pulp, paper, and textile industries.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2191-0855
Relation: https://doaj.org/toc/2191-0855
DOI: 10.1186/s13568-022-01472-0
URL الوصول: https://doaj.org/article/631f7d8b0c684bf1b48f7072a46ff307
رقم الأكسشن: edsdoj.631f7d8b0c684bf1b48f7072a46ff307
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:21910855
DOI:10.1186/s13568-022-01472-0