A phytase characterized by relatively high pH tolerance and thermostability from the shiitake mushroom Lentinus edodes.

ABSTRACT: A monomeric phytase with a molecular mass of 14 kDa was acquired from fresh fruiting bodies of the shiitake mushroom Lentinus edodes. The isolation procedure involved chromatography on DEAE-cellulose, CM-cellulose, Q-Sepharose, Affi-gel blue gel, and a final fast protein liquid chromatography-gel filtration on Superdex 75. The purified phytase demonstrated the unique N-terminal amino acid sequence DPKRTDQVN, which exhibited no sequence similarity with those of other phytases previously reported. It expressed its maximal activity at pH 5.0 and 37 °C. Phytase activity manifested less than 20% change in activity over the pH range of 3.0-9.0, considerable thermostability with more than 60% residual activity at 70 °C, and about 40% residual activity at 95°C. It displayed a wide substrate specif

SUBMITTER: Zhang GQ 

PROVIDER: S-EPMC3618926 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature