The Complete Genome Sequence of a Bacterial Strain with High Alkalic Xylanase Activity Isolated from the Sludge Near a Papermill

Chen, Si; Feng, Hao; Li, Xin; Chao, Han-Chieh; Wu, Jang‐Yen; Li, Jun; Zhu, Wenjun; Ding, Yan

doi:10.1007/s00284-020-02227-5

Cited by 2 publications

(1 citation statement)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…M. imperiale YD‐01 was isolated from the sludge near a papermill and preserved in our laboratory (Chen et al., 2020; Gan et al, 2018). All restriction enzymes and DNA polymerase were purchased from TaKaRa.…”

Section: Methodsmentioning

confidence: 99%

Molecular cloning and characterization of a novel xylanase from Microbacterium imperiale YD‐01

et al. 2021

Self Cite

View full text Add to dashboard Cite

Xylaneses are very common xylanolytic enzymes, which are widely used in food, papermaking, and other industries. In this study, a xylanase‐encoding gene xyn1923, which encodes a protein of 1352 amino acids, was identified through the whole genome analysis of Microbacterium imperiale YD‐01. Bioinformatics analysis showed that Xyn1923 only had maximum similarity of 37% with the reported xylanase from Alkalihalobacillus halodurans C‐125, indicating that Xyn1923 was a novel xylanase. The enzymatic properties of Xyn1923 were systematically analyzed after purification. The results showed that the specific activity of the enzyme was 10.582 ± 0.413 U/mg, while the optimum pH and temperature of the enzyme were 7.0 and 70°C, respectively. The enzyme is stable in the pH range of 6.0–9.0, and the enzyme activity could maintain more than 85% of the original activity after 16 hr incubation at pH 9.0. The enzyme activity is relatively stable in the range of 30–60°C, and its enzyme activity could maintain more than 89% of the original activity after treatment at 60°C for 30 min. Low concentrations (≤1 mM) of Co2+, Ba2+, Fe2+, and Fe3+ metal ions exerted a stimulatory effect on the activity of Xyn1923. And in contrast, high concentrations (≥2 mM) of the above metal ions inhibit the activity of Xyn1923. Mg2+, Ag+, Cu2+, Ca2+, Mn2+, and Pb2+ ions showed a negative effect on the activity of Xyn1923. Enzyme kinetic studies showed that Km and Vmax values for xylan were 7.842 ± 0.538 mg/ml and 15.208 ± 0.822 U/mg, respectively. Xyn1923 was found to be a weakly alkaline thermophilic xylanase through an enzymatic property analysis. Practical applications Xylanases are widely used in food and feed, biofuels, papermaking, and other industries. However, their use is limited by poor performance under the conditions of pH and temperature. Therefore, the discovery of xylanases with the capability of working efficiently at alkaline pH and high temperature is the priority for its industrial applications. In this study, a novel xylanase‐encoding gene xyn1923 from Microbacterium imperiale YD‐01 was cloned and heterologously expressed in Escherichia coli. Enzymatic properties of this novel xylanase were investigated, indicating that the robust thermal stability and alkali resistance of Xyn1923 make it a potential candidate for the food and paper industries.

show abstract

Section: Methodsmentioning

confidence: 99%