Molecular characterization of a Penicillium chrysogenum exo‐1,5‐α‐L‐arabinanase that is structurally distinct from other arabinan‐degrading enzymes

FEBS Letters

Sakamoto, Tatsuji²  Ihara, Hideshi¹  Kawasaki, Haruhiko²  Shibano, Asako¹  Kasai, Naoya²  Inui, Hiroshi² 

[1] Department of Earth and Life Sciences, College of Integrated Arts and Sciences, Osaka Prefecture University, Osaka 599-8531, Japan;Division of Applied Biochemistry, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, Osaka 599-8531, Japan

关键词: Exo-arabinanase;    Arabinobiose;    Nucleotide sequence;    Expression;    Penicillium chrysogenum;    CDS;    coding sequence;    CLM-PCR;    cassette ligation-mediated polymerase chain reaction;    DP;    degree of polymerization;    GH;    glycosyl hydrolase;    HCA;    hydrophobic cluster analysis;    HPAEC;    high-performance anion-exchange chromatography;    MBP;    maltose binding protein;   

DOI  :  10.1016/S0014-5793(04)00106-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The nucleotide sequence of the abnx cDNA gene, which encodes an exo-arabinanase (Abnx) of Penicillium chrysogenum 31B, was determined. Abnx was found to be structurally distinct from known arabinan-degrading enzymes based on its amino acid sequence and a hydrophobic cluster analysis. The protein in the protein database with the highest similarity to Abnx was the Neurospora crassa conserved hypothetical protein. The abnx cDNA gene product expressed in Escherichia coli catalyzed the release of arabinobiose from α-1,5-L-arabinan. The activity of the recombinant Abnx towards a series of arabino-oligosaccharides, as expressed by k _cat/K _m value, was greatest with arabinohexaose.

【 授权许可】

Unknown