Abstract：
:An intra-cellular beta-glucosidase was purified to homogeneity by gel filtration, ion exchange chromatography and HPGPLC from mycelial extract of Termitomyces clypeatus in the presence of the glycosylation inhibitor 2-deoxy-d-glucose. CD spectroscopy demonstrated that the purified enzyme exhibited alpha-helical conformation. MALDI-TOF identified the enzyme's molecular weight as 6688Daltons, but SDS-PAGE and immunoblotting indicated that the enzyme formed aggregates. The enzyme also showed unique properties of co-aggregation with sucrase in the fungus. The enzyme showed around 80% stability up to 60 degrees C and residual activity was 80-100% between pH ranges 5-8. The enzyme had higher specific activity against p-nitrophenyl-d-glucopyranoside than cellobiose and HPLC showed that the enzyme possesses transglycosylation activity and synthesizes cello-oligosaccharides by addition of glucose. The enzyme will be useful in synthetic biology to produce complex bioactive glycosides and to avoid chemical hazards. This is the first report of a beta-glucosidase enzyme with such a low monomeric unit size.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Pal S,Banik SP,Ghorai S,Chowdhury S,Khowala Sdoi
10.1016/j.biortech.2009.11.064subject
Has Abstractpub_date
2010-04-01 00:00:00pages
2412-20issue
7eissn
0960-8524issn
1873-2976pii
S0960-8524(09)01569-7journal_volume
101pub_type
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