Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 73, Issue 10, Pages 2303-2309Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90433
Keywords
arabinogalactan-protein; exo-beta-(1 -> 3)-galactanase; Irpex lacteus; Pichia pastoris; recombinant enzyme
Categories
Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [17770028]
- Grants-in-Aid for Scientific Research [17770028] Funding Source: KAKEN
Ask authors/readers for more resources
A gene encoding exo-beta-(1 -> 3)-galactanase from Irpex lacteus was cloned by reverse transcriptase-PCR. The deduced amino acid sequence showed high similarity with exo-beta-(1 -> 3)-galactanases from other sources. The molecular mass of the mature form was calculated to be 45,520 Da. The gene product expressed in Pichia pastoris specifically hydrolyzed beta-(1 -> 3)-galactooligosaccharides, as did other exo-beta-(1 -> 3)-galactanases. The recombinant enzyme showed high activity toward arabinogalactan-proteins (AGPs) from radish as well as beta-(1 -> 3)-galactan. Product analysis revealed that the enzyme released beta-(1 -> 6)-galactobiose, beta-(1 -> 6)-galactotriose, and alpha-L-arabinofuranosyl beta-(1 -> 3)-beta-galactosyl-beta-(1 -> 6)-galactose together with Gal from beta-(1 -> 3)-galactans attached with and without beta-(1 -> 6)-galactosyl branches prepared from acacia gum. These results indicate that the exo-beta-(1 -> 3)-galactanase from I. lacteus efficiently hydrolyzes beta-(1 -> 3)galactan main chains of AGPs by bypassing beta-(1 -> 6)-galactosyl side chains.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available