Characterization of glycoside hydrolase family 11 xylanase from Streptomyces sp. strain J103; its synergetic effect with acetyl xylan esterase and enhancement of enzymatic hydrolysis of lignocellulosic biomass SCIE SCOPUS

Cited 4 time in WEB OF SCIENCE Cited 5 time in Scopus
Title
Characterization of glycoside hydrolase family 11 xylanase from Streptomyces sp. strain J103; its synergetic effect with acetyl xylan esterase and enhancement of enzymatic hydrolysis of lignocellulosic biomass
Author(s)
Marasinghe, Svini Dileepa; Jo, Eunyoung; Hettiarachchi, Sachithra Amarin; Lee, Youngdeuk; Eom, Tae Yang; Gang, Yehui; Kang, Yoon Hyeok; Oh, Chulhong
KIOST Author(s)
Marasinghe, Svini Dileepa(Svini)Jo, Eunyoung(조은영)Lee, Young Deuk(이영득)Eom, Tae Yang(엄태양)Gang, Ye Hui(강예희)Oh, Chul Hong(오철홍)
Alternative Author(s)
Svini Dileepa Marasinghe; 조은영; Hettiarachchi Sachithra Amarin; 이영득; 엄태양; 강예희; 강윤혁; 오철홍
Publication Year
2021-07-08
Abstract
Background Xylanase-containing enzyme cocktails are used on an industrial scale to convert xylan into value-added products, as they hydrolyse the beta-1,4-glycosidic linkages between xylopyranosyl residues. In the present study, we focused on xynS1, the glycoside hydrolase (GH) 11 xylanase gene derived from the Streptomyces sp. strain J103, which can mediate XynS1 protein synthesis and lignocellulosic material hydrolysis. Results xynS1 has an open reading frame with 693 base pairs that encodes a protein with 230 amino acids. The predicted molecular weight and isoelectric point of the protein were 24.47 kDa and 7.92, respectively. The gene was cloned into the pET-11a expression vector and expressed in Escherichia coli BL21(DE3). Recombinant XynS1 (rXynS1) was purified via His-tag affinity column chromatography. rXynS1 exhibited optimal activity at a pH of 5.0 and temperature of 55 degrees C. Thermal stability was in the temperature range of 50-55 degrees C. The estimated K-m and V-max values were 51.4 mg/mL and 898.2 U/mg, respectively. One millimolar of Mn2+ and Na+ ions stimulated the activity of rXynS1 by up to 209% and 122.4%, respectively, and 1 mM Co2+ and Ni2+ acted as inhibitors of the enzyme. The mixture of rXynS1, originates from Streptomyces sp. strain J103 and acetyl xylan esterase (AXE), originating from the marine bacterium Ochrovirga pacifica, enhanced the xylan degradation by 2.27-fold, compared to the activity of rXynS1 alone when Mn2+ was used in the reaction mixture; this reflected the ability of both enzymes to hydrolyse the xylan structure. The use of an enzyme cocktail of rXynS1, AXE, and commercial cellulase (Celluclast (R) 1.5 L) for the hydrolysis of lignocellulosic biomass was more effective than that of commercial cellulase alone, thereby increasing the relative activity 2.3 fold. Conclusion The supplementation of rXynS1 with AXE enhanced the xylan degradation process via the de-esterification of acetyl groups in the xylan structure. Synergetic action of rXynS1 with commercial cellulase improved the hydrolysis of pre-treated lignocellulosic biomass; thus, rXynS1 could potentially be used in several industrial applications.
ISSN
1475-2859
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/41513
DOI
10.1186/s12934-021-01619-x
Bibliographic Citation
MICROBIAL CELL FACTORIES, v.20, no.1, 2021
Publisher
BMC
Subject
THERMOSTABLE XYLANASE; PURIFICATION; EXPRESSION; GENE; PADANUS; CLONING; FUNGICHROMIN; CELLULASE; MACROLIDE; SEQUENCE
Keywords
Xylanase; Streptomyces sp; strain J103; Expression; Purification; Synergism; Lignocellulosic biomass
Type
Article
Language
English
Document Type
Article
Publisher
BMC
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