Purification and biochemical characterization of an extracellular β-d-fructofuranosidase from Aspergillus sp.

ABSTRACT: This study focused on the purification and characterization of an extracellular β-d-fructofuranosidase or invertase from Aspergillus sojae JU12. The protein was purified by size exclusion chromatography with 5.41 fold and 10.87% recovery. The apparent molecular mass of the enzyme was estimated to be ~ 35 kDa using SDS-PAGE and confirmed by deconvoluted mass spectrometry. The fungal β-d-fructofuranosidase was suggested to be a monomer by native PAGE and zymography, and was found to be a glycoprotein possessing 68.92% carbohydrate content. The products of enzyme hydrolysis were detected by thin layer chromatography and revealed the monosaccharide units, d-glucose and d-fructose. β-d-fructofuranosidase showed enhanced activity at broad pH 4.0-9.0 and activity at a temperature range fro

SUBMITTER: Lincoln L 

PROVIDER: S-EPMC5794676 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature