[Purification, identification and characterization of an endoglucanase Egn20 from Fusarium sp. Q7-31T].

Autor:	Tian F, Xie Z, Guo J, Zhao L, Han X, Chang X
Jazyk:	čínština
Zdroj:	Wei sheng wu xue bao = Acta microbiologica Sinica [Wei Sheng Wu Xue Bao] 2015 Aug 04; Vol. 55 (8), pp. 1042-9.
Abstrakt:	Objective: The endoglucanase from Fusarium sp. Q7-31T was isolated, purified, identified and characterized to provide data for enzyme system of Fusarium sp. . [Methods] Strain was cultured in liquid fermentation with oat straw as carbon source, the endoglucanase was purified by using Sephacry S-100 chromatography and DEAE-sepharose ion-exchange column chromatography and the enzymatic properties were studied. The protein was identified using MADIL-TOF-TOF. Results: An endoglucanase was purified and named Egn20. The molecular weight was 55.37 kDa and isoelectric point (pI) was 7.44. Egn20 had optimal activity with carboxymethyl cellulose at 40 degrees C and pH 6.0, stabilized at 45 degrees C and pH 5.0 - 7.0, activated by Fe2+, inhibited by Na+, Ca2+, Mg2+, Zn2+, K+ and inactivated by Hg2+. The enzymatic properties and MADIL-TOF-TOF results suggested that Egn20 belongs to GH7 family. Conclusion: Our results may provide important data for the study of Fusarium sp. enzyme system.
Databáze:	MEDLINE
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