Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes faecalis T1 by using a quartz crystal microbalance.
Enzymatic adsorption and degradation of three types of aliphatic polyester films and two types of polyolefin films by the extracellular PHB depolymerase from Alcaligenes faecalis T1 have been studied by using a quartz crystal microbalance (QCM) technique. Hydrolysis of poly[(R)-3-hydroxybutyrate] was quantitatively followed by the QCM technique. Adsorption of the enzymes to films was also quantitatively detected by the QCM. Kinetic study on enzymatic adsorption suggests that the PHB depolymerase binds to the substrates not only by hydrophobic interaction but also by specific interaction between the ester bonds of polyesters and the binding domain of the enzyme. The results show that the QCM technique is a sensitive tool to study enzymatic degradation kinetics of biodegradable polyesters.
Yamashita
K
K
Polymer Chemistry Laboratory, RIKEN Institute, Hirosawa 2-1, Wako-shi, Saitama 351-0198, Japan. koyama@postman.riken.go.jp
Aoyagi
Y
Y
Abe
H
H
Doi
Y
Y
D000327:Adsorption; D000421:Alcaligenes / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D006885:Hydroxybutyrates / Q000378:metabolism; D007700:Kinetics; D011090:Polyenes / Q000378:metabolism; D011091:Polyesters / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011791:Quartz; D013997:Time Factors; D014894:Weights and Measures; D000094122:Polyhydroxybutyrates
D006026:Glycoside Hydrolases; D006885:Hydroxybutyrates; D011090:Polyenes; D011091:Polyesters; D011791:Quartz; C003182:poly-beta-hydroxybutyrate; D000094122:Polyhydroxybutyrates; C035051:PL 732