دورية أكاديمية
أعرض في EDS

Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9

التفاصيل البيبلوغرافية
العنوان: Identification and Characterization of a Novel Thermostable GDSL Lipase LipGt6 from Geobacillus thermoleovorans H9
المؤلفون: Lirong Qin, Min Lin, Yuhua Zhan, Shijie Jiang, Zhengfu Zhou, Jin Wang
المصدر: Applied Sciences, Vol 14, Iss 8, p 3279 (2024)
بيانات النشر: MDPI AG, 2024.
سنة النشر: 2024
المجموعة: LCC:Technology
LCC:Engineering (General). Civil engineering (General)
LCC:Biology (General)
LCC:Physics
LCC:Chemistry
مصطلحات موضوعية: Geobacillus thermoleovorans, GDSL lipase, LipGt6, thermostable, Technology, Engineering (General). Civil engineering (General), TA1-2040, Biology (General), QH301-705.5, Physics, QC1-999, Chemistry, QD1-999
الوصف: Lipases are versatile biocatalysts for various biological reactions. In the detergent industry, lipases must exhibit high activity in environments with high temperature, high pH values, metal ions, and organic solvents. Therefore, researchers are intensively searching for more stable and efficient lipases. A new thermophilic lipase, LipGt6, was identified in Geobacillus thermoleovorans H9, a new thermophilic strain isolated from ultrahigh-temperature compost. A structural model of LipGt6 was constructed using an esterase from Geobacillus thermodenitrificans as a template, and site-directed mutagenesis confirmed the predicted active site residues. LipGt6 exhibited the highest activity towards medium- and long-chain fatty acids (C8–C14), and the optimum temperature and pH were 50 °C and 9.0, respectively. LipGt6 was found to be thermostable up to 70 °C. In the presence of 1% H2O2 and sodium deoxycholate, LipGt6 retained 70 to 75% relative activity. These findings reveal that LipGt6 is potentially useful for the industrial production of detergent. Based on comparison of the amino acid sequences, the enzyme belongs to a new subfamily called lipolytic enzyme family II. The catalytic residues Ser and His were more critical than Asp, and the Asp221 catalytic residue is not likely critical for the lipolytic reaction of LipGt6.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2076-3417
Relation: https://www.mdpi.com/2076-3417/14/8/3279; https://doaj.org/toc/2076-3417
DOI: 10.3390/app14083279
URL الوصول: https://doaj.org/article/ec162db107f64dcab68a519c1bff16f3
رقم الأكسشن: edsdoj.162db107f64dcab68a519c1bff16f3
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20763417
DOI:10.3390/app14083279