Expression and characterization of the 42 kDa chitinase of the biocontrol fungus Metarhizium anisopliae in Escherichia coli.
Albeit Metarhizium anisopliae is the best-characterized entomopathogenic fungus, the role of some hydrolytic enzymes during host cuticle penetration has not yet been established. Three chitinase genes (chit1, chi2, chi3) from Metarhizium have already been isolated. To characterize the chitinase coded by the chit1 gene, we expressed the active protein (CHIT42) in Escherichia coli using a T7-based promoter expression vector. The recombinant protein, CHIT42, is active against glycol chitin and synthetic N-acetylglucosamine (GlcNAc) dimer and tetramer substrates. These activities suggest that the recombinant CHIT42 acts as an endochitinase.
Baratto
César Milton
CM
Centro de Biotechnologia, Universidade Federal do Rio Grande do Sul, UFRGS, Porto Alegre, RS, Brazil.
da Silva
Marcia Vanusa
MV
Santi
Lucélia
L
Passaglia
Luciane
L
Schrank
Irene Silveira
IS
Vainstein
Marilene Henning
MH
Schrank
Augusto
A
D002688:Chitinases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003470:Culture Media; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006999:Hypocreales / Q000201:enzymology* / Q000235:genetics; D010572:Pest Control, Biological; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D003470:Culture Media; D011994:Recombinant Proteins; D002688:Chitinases