Characterization of an acetyl xylan esterase from the marine bacterium Ochrovirga pacifica and its synergism with xylanase on beechwood xylan

Abstract

Background Acetyl xylan esterase plays an important role in the complete enzymatic hydrolysis of lignocellulosic materials. It hydrolyzes the ester linkages of acetic acid in xylan and supports and enhances the activity of xylanase. This study was conducted to identify and overexpress the acetyl xylan esterase (AXE) gene revealed by the genomic sequencing of the marine bacterium Ochrovirga pacifica . Results The AXE gene has an 864-bp open reading frame that encodes 287 aa and consists of an AXE domain from aa 60 to 274. Gene was cloned to pET-16b vector and expressed the recombinant AXE (rAXE) in Escherichia coli BL21 (DE3). The predicted molecular mass was 31.75 kDa. The maximum specific activity (40.08 U/mg) was recorded at the optimal temperature and pH which were 50 °C and pH 8.0, respectively. The thermal stability assay showed that AXE maintains its residual activity almost constantly throughout and after incubation at 45 °C for 120 min. The synergism of AXE with xylanase on beechwood xylan, increased the relative activity 1.41-fold. Conclusion Resulted higher relative activity of rAXE with commercially available xylanase on beechwood xylan showed its potential for the use of rAXE in industrial purposes as a de-esterification enzyme to hydrolyze xylan and hemicellulose-like complex substrates. Electronic supplementary material The online version of this article (10.1186/s12934-019-1169-y) contains supplementary material, which is available to authorized users.

A genomic view of the microbiome of coral reef demosponges

“…xylans). Characterisation of CE15 and CE7 from marine microbes is rare, though activity on xylans, which are a structural component of marine algae, has previously been demonstrated [ 55 – 57 ].

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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

“…Several studies on the synergism between xylanases and acetyl xylan esterases reported by Hettiarachchi et al and Yang et al [ 19 , 38 ] showed the removal of acetyl groups in xylan and improvement in xylan hydrolysis. Experiments were performed to investigate the synergetic effect of XynS1 derived from Streptomyces sp.…”

“…AXE derived from the marine bacteria O. pacifica was used to investigate the synergetic effect with rXynS1 on xylan hydrolysis. According to the results of conserved domain analysis, the AXE derived from O. pacifica has been classified under the alpha/beta hydrolase family [ 19 ]. Mn 2+ was used in the experiment as Mn 2+ can improve the enzymatic activities of rXynS1 and AXE.…”

“…It was used in the cloning, expression, and biochemical characterisation processes. The synergetic effect of xylanase enzyme was detected with AXE originating from marine bacteria, O. pacifica reported by Hettiarachchi et al [ 19 ]. Further experiments were designed to determine the synergetic action of enzyme cocktails on pre-treated lignocellulosic biomass hydrolysis.…”

“…Over the last decade, xylanase has attracted attention because it can potentially be used in various industrial processes for food, pulp, paper, and biofuel production [ 17 , 18 ]. Xylanases with commercial value have reportedly been derived from marine and terrestrial bacteria, actinomycetes, and fungi [ 19 ]. It is well known that the genus Streptomyces is used for the production of commercially available antibiotics [ 20 ] and enzymes [ 21 ]; these organisms are recognised as being lignocellulosic [ 22 ] and chitin degraders [ 23 ].…”