Ontology type: schema:ScholarlyArticle
2013-10
AUTHORSYukiko Shinozaki, Yoshihiro Kikkawa, Shun Sato, Tokuma Fukuoka, Takashi Watanabe, Shigenobu Yoshida, Toshiaki Nakajima-Kambe, Hiroko K. Kitamoto
ABSTRACTEnzymatic degradation of polyester films by a cutinase-like enzyme from Pseudozyma antarctica JCM10317 (PaE) was analyzed by surface plasmon resonance (SPR). The adsorption of PaE and the degradation rate for polyester films were quantitatively monitored by a positive and negative SPR signal shifts, respectively. The decrease in SPR signal and the erosion depth of amorphous poly(L-lactide) (a-PLLA) film measured by atomic force microscopy (AFM) had a linear relationship, and the weight loss was estimated from the AFM data combined with a density of a-PLLA film. Furthermore, SPR sensorgrams for various polyester films showed that degradation rate of poly(ε-caprolactone) and poly(butylene succinate-co-adipate) which contain C6 units was higher than that of other polyesters such as poly(butylene succinate) and a-PLLA. These results suggest that C6 is the preferred chain length as substrates for PaE. More... »
PAGES8591-8598
http://scigraph.springernature.com/pub.10.1007/s00253-012-4673-0
DOIhttp://dx.doi.org/10.1007/s00253-012-4673-0
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/23339012
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