Biomaterial Database

Preparation, purification and characteristics of an aflatoxin degradation enzyme from Myxococcus fulvus ANSM068. 2011

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

National Laboratory of Animal Nutrition, College of Animal Science & Technology, China Agricultural University, Beijing, China.

OBJECTIVE 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. 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. CONCLUSIONS 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.

UI	MeSH Term	Description	Entries
D000348	Aflatoxins	Furano-furano-benzopyrans that are produced by ASPERGILLUS from STERIGMATOCYSTIN. They are structurally related to COUMARINS and easily oxidized to an epoxide form to become ALKYLATING AGENTS. Members of the group include AFLATOXIN B1; aflatoxin B2, aflatoxin G1, aflatoxin G2; AFLATOXIN M1; and aflatoxin M2.	Aflatoxin
D001426	Bacterial Proteins	Proteins found in any species of bacterium.	Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D016604	Aflatoxin B1	A potent hepatotoxic and hepatocarcinogenic mycotoxin produced by the Aspergillus flavus group of fungi. It is also mutagenic, teratogenic, and causes immunosuppression in animals. It is found as a contaminant in peanuts, cottonseed meal, corn, and other grains. The mycotoxin requires epoxidation to aflatoxin B1 2,3-oxide for activation. Microsomal monooxygenases biotransform the toxin to the less toxic metabolites aflatoxin M1 and Q1.	Aflatoxin B(1),Aflatoxin B,Aflatoxin B1 Dihydrochloride, (6aR-cis)-Isomer,Aflatoxin B1, (6aR-cis)-Isomer, 14C-Labeled,Aflatoxin B1, (6aR-cis)-Isomer, 2H-Labeled,Aflatoxin B1, (6aR-cis)-Isomer, 3H-Labeled,Aflatoxin B1, cis(+,-)-Isomer,HSDB-3453,NSC-529592,HSDB 3453,HSDB3453,NSC 529592,NSC529592
D016607	Aflatoxin M1	A 4-hydroxylated metabolite of AFLATOXIN B1, one of the MYCOTOXINS from ASPERGILLUS tainted food. It is associated with LIVER damage and cancer resulting from its P450 activation to the epoxide which alkylates DNA. Toxicity depends on the balance of liver enzymes that activate it (CYTOCHROME P-450) and others that detoxify it (GLUTATHIONE S TRANSFERASE) (Pharmac Ther 50.443 1991). Primates & rat are sensitive while mouse and hamster are tolerant (Canc Res 29.236 1969).	Aflatoxin M(1),4-Hydroxyaflatoxin B1,Aflatoxin M,Aflatoxin M1, cis(+-)-Isomer,4 Hydroxyaflatoxin B1
D016940	Myxococcus	A genus of gliding bacteria that are common inhabitants on tree bark and decomposing vegetation. The cells are slender rods with tapering ends.