[논문]Cloning and heterologous expression of xylanase from Pichia stipitis in Escherichia coli

Basaran, P.; Hang, Y.D.; Basaran, N.; Worobo, R.W.

doi:10.1046/j.1365-2672.2001.01237.x

Cloning and heterologous expression of xylanase from Pichia stipitis in Escherichia coli

Journal of applied microbiology, v.90 no.2, 2001년, pp.248 - 255

Basaran, P. , Hang, Y.D. , Basaran, N. , Worobo, R.W.

Abstract ▼ AI-Helper

AIMS: The main goal of this study was to characterize the xylanase (xynA) gene from Pichia stipitis NRRL Y-11543. METHODS AND RESULTS: The xylanase gene was cloned into pUC19 in Escherichia coli DH5alphaF' and selected by growth on RBB-xylan. All functional clones contained a recombinant plasmid with an insert of 2.4 kbp, as determined by restriction mapping. The nucleotide sequence of the P. stipitis xylanase gene consisted of 1146 bp and encoded a protein of 381 amino acids with a molecular weight of 43 649 Da. The sequence contained a putative 20-amino acid N-terminal signal sequence and four N-linked glycosylation sites. The Km values for non-glycosylated and glycosylated xylanases were 1.4 mg ml-1 and 4.2 mg ml-1, respectively, and Vmax values were 0.8 and 0.082 micromol min-1 mg-1 protein, respectively. CONCLUSION: Xylanase, a rarely found enzyme in yeast species, has been characterized in detail. SIGNIFICANCE AND IMPACT OF THE STUDY: The results of this study can be used to develop better xylanase-utilizing yeast strains.

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동의어: Packet Collision Rate

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Cloning and heterologous expression of xylanase from Pichia stipitis in Escherichia coli

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참고문헌 (49)

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