Purification and Characterization of β-mannanase atMAN47 from Armillariella tabescens

Abstract:

Armillariella. tabescens EJLY2098 was induced to produce β-mannanase with konjac fine flour (Amorphopallus rivieri) as single carbon source. This induced enzyme was then purified using DEAE ion exchange chromatography and named atMAN47. Zymologic analysis showed that the molecular weight of this β-mannanase was approximately 47 kD. The enzyme was stable when pH ranged from 5.0 to 6.5 and could be activated by Na+ and Ba2+. With an optimal temperature of 50°C. Action mode analysis of TLC re-vealed that the enzyme belonged to the endo-β-mannanase family. Being a meta-acid endo-β-mannanase, it was suitable to be applied to feed industry with a promising future as an enzyme preparation.