Molecular cloning and characterization of a novel alpha-galactosidase gene from Penicillium sp F63 CGMCC 1669 and expression in Pichia pastoris

文献类型： 外文期刊

第一作者： Mi, Shijun

作者： Mi, Shijun;Meng, Kun;Wang, Yaru;Bai, Yingguo;Yuan, Tiezheng;Luo, Huiying;Yao, Bin

作者机构：

关键词： alpha-galactosidase;Penicillium sp.;molecular cloning;gene expression;Pichia pastoris

期刊名称：ENZYME AND MICROBIAL TECHNOLOGY （ 影响因子：3.493； 五年影响因子：3.699 ）

ISSN： 0141-0229

年卷期： 2007 年 40 卷 5 期

页码：

收录情况： SCI

摘要： An extracellular alpha-galactosidase (EC 3.2.1.22) from Penicillium sp. F63 CGMCC 1669, designated Agl1, was purified to homogeneity by means of fast protein liquid chromatography (FPLC) with a molecular mass of 82 kDa on SDS-PAGE while 330 kDa on native gradient PAGE. Based on the partial amino acid sequences of the purified protein, Agl1 gene encoding the alpha-galactosidase was cloned and sequenced. The ORF of Agl1 consisted of 2205 nucleotides encoding a protein of 735 amino acids including 21 residues of a putative signal peptide in its N-terminal. Agl1 was intron-less, and a GUG codon was considered the start codon of the gene. Agl1 possessed the highest sequence identity of 69.5% with alpha-galactosidase AglC from Aspergillus niger and showed a little homology to those of Penicillum purpurogenum and Penicillium simplicissimum reported previously, namely, 7.5% and 8.0%, respectively. The mature protein had been expressed extracellularly in Pichia pastoris with a yield of 111 U/ml in a 3-1 fermenter. The optimum pH and temperature of the recombinant a-galactosidase were 5.0 and 40 degrees C, respectively. The recombinant alpha-galactosidase hydrolyzed the release of galactose from natural oligosaccharides, such as melibiose, raffinose, and stachyose. To our knowledge, this is the first report of gene cloning for Penicillium alpha-galactosidase belonging to family 36 of glycosyl hydrolases and expression in Pichia pastoris. (c) 2006 Elsevier Inc. All rights reserved.

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