Literature DB >> 11749150

Analysis of adsorption function of polyhydroxybutyrate depolymerase from Alcaligenes faecalis T1 by using a quartz crystal microbalance.

K Yamashita1, Y Aoyagi, H Abe, Y Doi.   

Abstract

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.

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Year:  2001        PMID: 11749150     DOI: 10.1021/bm0000844

Source DB:  PubMed          Journal:  Biomacromolecules        ISSN: 1525-7797            Impact factor:   6.988


  2 in total

1.  Effects of mutations in the substrate-binding domain of poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation.

Authors:  Tomohiro Hiraishi; Yoko Hirahara; Yoshiharu Doi; Mizuo Maeda; Seiichi Taguchi
Journal:  Appl Environ Microbiol       Date:  2006-09-08       Impact factor: 4.792

2.  Enhanced degradation of polyhydroxyalkanoates (PHAs) by newly isolated Burkholderia cepacia DP1 with high depolymerase activity.

Authors:  Nor Azura Azami; Ira Aryani Wirjon; Shantini Kannusamy; Aik-Hong Teh; Amirul Al-Ashraf Abdullah
Journal:  3 Biotech       Date:  2017-04-27       Impact factor: 2.406

  2 in total

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