Purification and characterization of endoglucanase Egn21 from Fusarium sp. Q7-31T

Abstract:

Abstract: [Objective] The objective of this research was to study plant cell wall degradation enzymes from Fusarium sp. Q7-31T. [Methods] Strain was cultured in liquid medium with 1% (W/V) peptone as nitrogen source, 0.5% (W/V) oat straw as carbon source, 120 r/min shaking at 20 °C for 3 days. The endoglucanase Egn21 was purified by using Sephacry S-100 chromatography and DEAE-sepharose ion-exchange column chromatography. Then the enzymatic properties and MADIL-TOF-TOF identification were analyzed. [Results] The molecular weight and isoelectric point (pI) of Egn21 was 44.25 kDa and 4.91, respectively. Egn21 had optimal activity with carboxymethyl cellulose at 40 °C and pH 6.0, stable at 45 °C and pH between 5.0 and 8.0, inhibited by Fe2+, Ca2+, K+, Na+, Mn2+ and inactivated by Hg2+, whereas Co2+, Zn2+ and Mg2+ had no effect. [Conclusion] The enzymatic properties and MADIL-TOF-TOF results suggested that Egn21 belongs to GH5 family.

Key words:Keywords: Fusarium sp., endoglucanase, protein purification, identification, enzymatic properties