Products/Services Used | Details | Operation |
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Proteins, Expression, Isolation and Analysis> | Then, the expressed protein was pur- ified using High Affinity Ni-Charged Resin FF (GenScript, China) ac- cording to the manufacturer’s instructions. | Get A Quote |
A novel β-1,3-glucanase from Arca inflata was purified using chromatography methods. It was determined as a glycoprotein comprising 23.65% carbohydrate content with O-linked glycan and showed specific activity of 90.01?±?1.2?U/mg against laminarin. The optimal pH and temperature for the activity of the glucanase were 6.0 and 40?°C, respectively. The affinity parameter of the glucanase using laminarin was determined as K?=?13.09?μM. The activity of the glucanase was 27?±?2.6% enhanced by 2-mM Mn ions and inhibited by 40-50% using 2-mM Zn, Cu, or Ba ions. The glucanase showed an endo-type cleavage mode and hydrolyzed laminarin into glucoses, disaccharides, trioligosaccharides, and tetraoligosac... More