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- Title
Characterization of a Thermostable Family 1 Glycosyl Hydrolase Enzyme from Putranjiva roxburghii Seeds.
- Authors
Patel, Girijesh; Kar, Bibekananda; Sharma, Ashwani
- Abstract
A 66-kDa thermostable family 1 Glycosyl Hydrolase (GH1) enzyme with β-glucosidase and β-galactosidase activities was purified to homogeneity from the seeds of Putranjiva roxburghii belonging to Euphorbiaceae family. N-terminal and partial internal amino acid sequences showed significant resemblance to plant GH1 enzymes. Kinetic studies showed that enzyme hydrolyzed p-nitrophenyl β- d-glucopyranoside ( pNP-Glc) with higher efficiency ( K/ K = 2.27 × 10 M s) as compared to p-nitrophenyl β- d-galactopyranoside ( pNP-Gal; K/ K = 1.15 × 10 M s). The optimum pH for β-galactosidase activity was 4.8 and 4.4 in citrate phosphate and acetate buffers respectively, while for β-glucosidase it was 4.6 in both buffers. The activation energy was found to be 10.6 kcal/mol in the temperature range 30-65 °C. The enzyme showed maximum activity at 65 °C with half life of ~40 min and first-order rate constant of 0.0172 min. Far-UV CD spectra of enzyme exhibited α, β pattern at room temperature at pH 8.0. This thermostable enzyme with dual specificity and higher catalytic efficiency can be utilized for different commercial applications.
- Subjects
ENZYMES; GLUCOSIDASES; GALACTOSIDASES; EUPHORBIACEAE; AMINO acids
- Publication
Applied Biochemistry & Biotechnology, 2012, Vol 166, Issue 3, p523
- ISSN
0273-2289
- Publication type
Academic Journal
- DOI
10.1007/s12010-011-9445-2