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Article: Molecular Cloning of a [beta]-Galactosidase from Radish That Specifically Hydrolyzes [beta]-(1[arrow right]3)- and [beta]-(1[arrow right]6)-Galactosyl Residues of Arabinogalactan Protein1
- Article from:
- Plant Physiology
- Article date:
- July 1, 2005
- Author:
CopyrightCopyright American Society of Plant Physiologists Jul 2005. Provided by ProQuest LLC. (Hide copyright information)
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A basic β-galactosidase with high specificity toward β-(1[arrow right]3)- and β-(1[arrow right]6)-galactosyl residues was cloned from radish (Raphanus sativus) plants by reverse transcription-PCR. The gene, designated RsBGAL1, contained an open reading frame consisting of 2,532 bp (851 amino acids). It is expressed in hypocotyls and young leaves. RsBGAL1 was highly similar to β-galactosidases having exo-β-(1[arrow right]4)-galactanase activity found in higher plants and belongs to family 35 of the glycosyl hydrolases. Recombinant RsBGAL1 was expressed in Pichia pastoris and purified to homogeneity. The recombinant enzyme specifically hydrolyzed β-(1[arrow ...