Characteristics of recombinant xylanase from camel rumen metagenome and its effects on wheat bran hydrolysis.

In the present study, we explored the effects of a novel xylanase from camel rumen metagenome (CrXyn) on wheat bran hydrolysis. CrXyn was heterologously expressed in Escherichia coli and showed maximum activity at 40 °C and pH 7.0. Furthermore, CrXyn exhibited preferential hydrolysis of xylan, but no obvious activity toward other substrates, including carboxymethylcellulose and Avicel. Using wheat straw xylan as a substrate, the Km and Vmax values for CrXyn were 5.98 g/L and 179.9 μmol xylose/min/mg protein, respectively. Mn ²⁺ was a strong accelerator and significantly enhanced CrXyn activity. However, CrXyn activity was inhibited (~50 %) by 1 mM and 5 mM ethylenediaminetetraacetic acid (EDTA) and completely inactivated by 5 mM Cu ²⁺ . CrXyn tolerated 5 mM sodium dodecyl sulphate (SDS) and 15 % methanol, ethanol, and dimethyl sulfoxide (DMSO), with >50 % residual activity. CrXyn effectively hydrolyzed wheat bran, with xylobiose and xylotetraose accounting for 79.1 % of total sugars produced. A remarkable synergistic effect was found between CrXyn and protease, leading to an obvious increase in amino acids released from wheat bran compared with the control. CrXyn also enhanced the in vitro hydrolysis of wheat bran. Thus, CrXyn exhibits great potential as a feed additive to improve the utilization of wheat bran in monogastric animal production.
Competing Interests: Declaration of competing interest The authors declare no conflict of interest.
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