Identification and characterization of a novel endo-β-1, 4-glucanase from a soil metagenomic library. (December 2021)

• Record Type: Journal Article
• Authors: Chai, Shumao; Zhang, Xueliang; Gao, Yuejiao; Nie, Lishuang; Xiang, Chenchen; Cao, Mingming; Wang, Shaochen; Feng, Zhiyang
• Is Part Of: Carbohydrate research. Volume 510(2021)
• Publication Date: 2021-12
• Subjects: Functional metagenomics -- endo-β-1, 4-Glucanase -- Glycoside hydrolase family 6 -- Transmembrane region; Carbohydrates -- Periodicals; Chemistry, Organic -- Periodicals; Biochemistry -- Periodicals; Carbohydrates -- Periodicals; Chimie organique -- Périodiques; Glucides -- Périodiques; Biochemistry; Carbohydrates; Chemistry, Organic; Periodicals; Electronic journals; 507.78
• DOI: 10.1016/j.carres.2021.108460
• Languages: English
• ISSNs: 0008-6215

Abstract

Abstract: A cosmid clone cZFYN1413 with CMCase activity was identified from a soil metagenomic library. The sequence analysis of a subclone of cZFYN1413 revealed an endo- β -1, 4-glucanase gene ZFYN1413 belonging to glycoside hydrolase family 6 and a transmembrane region in the N-terminal of ZFYN1413. Expression of ZFYN1413 in Escherichia coli BL21 (DE3) resulted in ZFYN1413-87, which was a truncated protein cleaved in transmembrane region of ZFYN1413. ZFYN1413-87 was expressed and its enzyme properties were studied. ZFYN1413-87 possessed strong endo-β-1, 4-glucanase activity, and 52% of the activity could be retained after the protein was treated in buffer of pH 3.0 for 2 h. The study provided a special example of endo- β -1, 4-glucanase in GH6 family. Graphical abstract: Image 1 Highlights: A novel endo- β -1, 4-glucanase was identified from a soil metagenomic library. The enzyme is stable at pH 3.0-9.0 and 20-40°C. Cellulase self-cleaved from the transmembrane region during the protein processing. The novel enzyme provides a special example of cellulase in glycoside hydrolase family 6.