A Phytase Characterized by Relatively High pH Tolerance and Thermostability from the Shiitake Mushroom Lentinus edodes
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AbstractA 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 degrees 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 degrees C, and about 40% residual activity at 95 degrees C. It displayed a wide substrate specificity on a variety of phosphorylated compounds with the following ranking: ATP > fructose-6-phosphate > AMP > glucose-6-phosphate > ADP > sodium phytate > beta-glycerophosphate. The phytase activity was moderately stimulated by Ca2+, but inhibited by Al3+, Mn2+, Zn2+, and Cu2+ at a tested concentration of 5 mM.
All Author(s) ListZhang GQ, Wu YY, Ng TB, Chen QJ, Wang HX
Journal nameBioMed Research International
Detailed descriptionTo ORKTS: doi: 10.1155/2013/540239
PublisherHindawi Publishing Corporation
LanguagesEnglish-United Kingdom
Web of Science Subject CategoriesBiotechnology & Applied Microbiology; Medicine, Research & Experimental; Research & Experimental Medicine

Last updated on 2021-06-05 at 01:22