[Purification, identification and characterization of an endoglucanase Egn20 from Fusarium sp. Q7-31T]
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High Throughput Screening of Fungal Endoglucanase Activity in Escherichia coli
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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.
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