Cutin, a polymeric structural component of plant cuticles, is a polymer of hydroxy fatty acids that are usually C16 or C18 and contain up to three hydroxy groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
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SYSTEMATIC NAME
IUBMB Comments
cutin hydrolase
Cutin, a polymeric structural component of plant cuticles, is a polymer of hydroxy fatty acids that are usually C16 or C18 and contain up to three hydroxy groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
cutinase is an esterase, whose active site, located at the middle of a sharp turn between beta-strand and alpha-helix, is composed by the triad Ser120, Asp175 and His188
cutinase catalyzes esterification of caproic acid in an organic solvent system, alcohol, acid and n-decane are mixed thoroughly in iso-octane before the addition of the lyophilized enzyme, overview. The main kinetic characteristics observed in esterification reaction follow an ordered Ping-Pong Bi-Bi mechanism
cutinase is an esterase, whose active site, located at the middle of a sharp turn between beta-strand and alpha-helix, is composed by the triad Ser120, Asp175 and His188
site-directed mutagenesis, the mutant shows transesterification activity similar to the wild-type enzyme, T179C displays high stability in the presence of methanol with an activity loss of only 16% as compared to 90% loss of wild-type activity, the mutant is also more stable microencapsulated in reversed micelles of bis(2-ethylhexyl) sodium sulfosuccinate in isooctane
cutinase is microencapsulated in reversed micelles of bis(2-ethylhexyl) sodium sulfosuccinate in isooctane for the production of alkyl esters, known as biodiesel, evaluation of the system stability using wild-type enzyme and three mutants, L153Q, T179C and S54D, method evaluation, overview. Loss of 45% of wild-type cutinase activity when incubated in the micellar system for 3 h, and an additional loss of 90% of the activity is observed in the presence of methanol after 10 min of incubation
stability of the cutinase in different organic solvents. The cutinase is incubated with 75% v/v of organic solvent in assay buffer at 20°C for 18 h, overview
study of enzyme partition in a 20% polyethylene glykol/15% phosphate two-phase system. Specific interaction of butyrate to the active site of enzyme, enzyme-butyrate complex is over two times the size of the free enzyme
adsorption of enzyme onto the surface of poly(methyl methacrylate) latex particles. Up to 50% decrease in specific activity at pH-values 4.5 and 5.2. Almost no inactivation upon adsorption at pH 7.0 and 9.2. 60% increase in maximum adsorption with temperature raising from 25 to 50°C
immobilization of enzyme on sodium form of zeolite Y, half-life 590 days at 30°C. Immobilization on zolite A, halft-life of 54 days at 30°C. Half-lives after immobilization on Alumina and Accurel-PA6 are 109 and 10 days, resp. Higher temperatures induce a remarkable stability loss in all preparations. At 30°C, enzymatic activities obtained wit the immobilization on zeolite A are the highest ones
study on enzyme encapsulated in sol-gel matrices prepared with alkyl-alkoxysilane precursors of different chain length. Specific activity of entrapped enzyme is comparable to enzyme immobilized on zeolite Y, with incorporation of different additives bringing about an enhancement of enzyme activity and operational stability
a high enzyme production, high specific enzyme activity, and high enzyme yield are obtained upon expression with a 5% air saturation of oxygen. At low dissolved oxygen concentration, enzyme yield and specific activity increase with increase of culture pH-value from 5.25 to 6.25
recombinant cutinase from Fusarium solani pisi is used as a catalyst in enzymatic transesterification between a mixture of triglyceride oils and methanol for biodiesel production in a bis(2-ethylhexyl) sodium sulfosuccinate (AOT)/isooctane reversed micellar system, kinetics, overview