A heat inducible tyrosinase with distinct properties from Bacillus thuringiensis.
OBJECTIVE
The objective of this work was to purify the tyrosinase from Bacillusthuringiensis subsp. kurstaki (Bt) (CCTCC AB 90010) and study its enzymatic properties.


RESULTS
A 'one-step' purification method was used in this work, which was an easy, high-yield purification method. Tyrosinase activity of this purity was measured under different conditions to study its kinetic characterizations. The optimum pH and thermal stability of this enzyme were also determined. The results revealed that the tyrosinase from Bt has distinct properties compared with those from other sources.


CONCLUSIONS
A heat-inducible tyrosinase of a wild strain of Bt was identified and partially characterized.


CONCLUSIONS
The distinct properties of Bt tyrosinase are important to the application of Bt as a biology pesticide.
College of Life Sciences, Wuhan University, Wuhan, China.
N
N
Liu
T
T
Zhang
Y J
YJ
Wang
Y P
YP
Huang
J H
JH
Ou
P
P
Shen
D001413:Bacillus thuringiensis / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D004790:Enzyme Induction; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D014442:Monophenol Monooxygenase / Q000302:isolation & purification* / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
D008670:Metals; D014442:Monophenol Monooxygenase