Soluble expression of a novel feruloyl esterase from Burkholderia pyrrocinia B1213 in Escherichia coli and optimization of production conditions. Issue 1 (1st January 2020)

• Record Type: Journal Article
• Authors: Fu, Zhilei; Fan, Guangsen; Zhu, Yuting; Teng, Chao; Li, Hehe; Liu, Qian; Yang, Ran; Li, Xiuting
• Is Part Of: Biotechnology, biotechnological equipment. Volume 34:Issue 1(2020)
• Page Start: 732
• Page End: 746
• Publication Date: 2020-01-01
• Subjects: Burkholderia pyrrocinia -- feruloyl esterase -- optimization -- pGEX-4T-1 -- soluble expression; Biotechnology -- Periodicals; Biotechnology -- Periodicals; Biotechnology -- instrumentation -- Periodicals; Periodicals; 660.605
• DOI: 10.1080/13102818.2020.1803129
• Languages: English
• ISSNs: 1310-2818

Abstract

Abstract: This report examines the soluble expression of a novel feruloyl esterase, BpFae, from Burkholderia pyrrocinia in Escherichia coli overexpression systems using three expression vectors, pET28a, pCold-TF and pGEX-4T-1. BpFae was overexpressed as insoluble inclusion bodies when pET28a was used as the expression vector. BpFae was overexpressed in the soluble form when using pCold-TF; however, the overexpressed protein showed negligible activity. Recombinant BpFae was produced in the soluble form and active when E. coli cells were transformed with the pGEX-4T-1-BpFae vector. Optimal conditions for soluble overexpression of recombinant BpFae were determined, and the highest activity of recombinant BpFae was 2.54 U mL −1 . Multiple sequence alignment, phylogenetic analysis and construction of a three-dimensional model indicated that BpFae is a unique FAE from B. pyrrocinia with underlying research value.