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A novel xylanase from Streptomyces sp. FA1: Purification, characterization, identification, and heterologous expression

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Abstract

A xylanase (XynA) was purified from the culture medium of Streptomyces sp. FA1, which was previously isolated from a bamboo retting system. XynA had a molecular mass of 43 kDa, displayed maximal activity at pH 5.5, retained 41% of its maximal activity at pH 11.0, and was stable over a wide pH range (3.0 ∼ 11.0). Purified XynA was subjected to peptide mass fingerprinting, which led to the cloning of the xynA gene. The xynA gene, which encodes a mature protein of 436 amino acids, was heterologously expressed in E. coli BL21(DE3). The activity in the culture medium could reach 213.5 U/mL, which was 11.2-fold higher than that produced by Streptomyces sp. FA1. BLAST searching revealed that full-length XynA shares less than 90% identity with most of its homologues, whereas amino acids 48-436 of the enzyme share 97% identity with an open reading frame encoding a putative full-length mature xylanase from Streptomyces tendae. The truncated xynA gene, xynA 48-436, was cloned and expressed in E. coli, however, no xylanase activity could be detected in the culture medium. Based on these results, it is suggested that XynA is a new member of glycoside hydrolases family10 with exceptional catalytic efficiency at alkaline pH.

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Correspondence to Jing Wu.

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He, J., Su, L., Sun, X. et al. A novel xylanase from Streptomyces sp. FA1: Purification, characterization, identification, and heterologous expression. Biotechnol Bioproc E 19, 8–17 (2014). https://doi.org/10.1007/s12257-013-0490-2

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  • DOI: https://doi.org/10.1007/s12257-013-0490-2

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