Literature DB >> 21040271

Preparation, purification and characteristics of an aflatoxin degradation enzyme from Myxococcus fulvus ANSM068.

L H Zhao1, S Guan, X Gao, Q G Ma, Y P Lei, X M Bai, C Ji.   

Abstract

AIMS: To prepare, purify and characterize an extracellular enzyme from Myxococcus fulvus ANSM068, designated as myxobacteria aflatoxin degradation enzyme (MADE), which possesses degradation activity against aflatoxin B(1) (AFB(1) ), G(1) (AFG(1) ) and M(1) (AFM(1) ) in solution. METHODS AND
RESULTS: The culture supernatant of strain M. fulvus demonstrated high degradation ability against AFB(1) (71·89%), AFG(1) (68·13%) and AFM(1) (63·82%) after 48 h of incubation. An enzyme was purified from the supernatant of M. fulvus using ethanol precipitation and chromatography on DEAE-Sepharose and Superdex 75. An overall 166-fold purification of the enzyme with a recovery of 57% and a final specific activity of 569·44 × 10(3) U mg(-1) was obtained using the present purification protocol. The apparent molecular mass of MADE was estimated to be 32 kDa by SDS-PAGE. AFG(1) and AFM(1) were significantly degraded, by 96·96 and 95·80%, respectively, when treated with pure MADE (100 U ml(-1) ) produced by strain ANSM068. MADE exhibited the largest amount of activity at 35°C and pH 6·0, with Mg(2+) ions greatly promoting and Zn(2+) strongly inhibiting MADE activity.
CONCLUSIONS: An aflatoxin DEGRADATION ENZYME FROM BACTERIAL ISOLATES CAN EFFECTIVELY REMOVE AFLATOXIN B(1) , G(1) AND M(1) IN SOLUTION. SIGNIFICANCE AND IMPACT OF THE STUDY: The high activity and wide temperature and pH range of MADE for the degradation of aflatoxin have promising applications in control of mycotoxins during food and feed processing.
© 2010 The Authors. Journal of Applied Microbiology © 2010 The Society for Applied Microbiology.

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Year:  2010        PMID: 21040271     DOI: 10.1111/j.1365-2672.2010.04867.x

Source DB:  PubMed          Journal:  J Appl Microbiol        ISSN: 1364-5072            Impact factor:   3.772


  24 in total

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