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A Heterogeneous Kinetic Model for the Cutinase‐Catalyzed Hydrolysis of Cyclo‐tris‐ethylene Terephthalate
Author(s) -
Figeroa Yalitza,
Hinks David,
Montero Gerardo
Publication year - 2006
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp050309s
Subject(s) - cutinase , crystallinity , hydrolysis , ethylene , trimer , substrate (aquarium) , chemistry , reaction rate constant , tris , polyester , kinetics , aqueous solution , polymer chemistry , catalysis , organic chemistry , crystallography , biochemistry , dimer , oceanography , physics , quantum mechanics , geology
Abstract The kinetics of enzyme‐catalyzed hydrolysis of the polyester oligomer cyclo‐tris‐ethylene terephthalate, commonly known as cyclic trimer, using a developmental cutinase is reported. The effect of substrate surface area and enzyme concentration, in a largely aqueous medium, on the rate of hydrolysis was measured via spectrophotometric measurement using high performance liquid chromatography (λ 254 nm) at 60 °C in a glycine buffer (pH 8). The rate was strongly dependent on the substrateapos;s surface characteristics. When the substrate surface area was relatively small and the substrate was relatively low in crystallinity, the reaction followed zero order kinetics, whereas a first order rate constant was obtained when the substrate surface area was increased considerably and the crystallinity was relatively high.