Literature DB >> 15928850

Hydrolysis of polyesters by serine proteases.

Hyun-A Lim1, Takao Raku, Yutaka Tokiwa.   

Abstract

The substrate specificity of alpha-chymotrypsin and other serine proteases, trypsin, elastase, proteinase K and subtilisin, towards hydrolysis of various polyesters was examined using poly(L-lactide) (PLA), poly(beta-hydroxybutyrate) (PHB), poly(ethylene succinate) (PES), poly(ethylene adipate) (PEA), poly(butylene succinate) (PBS), poly(butylene succinate-co-adipate) (PBS/A), poly[oligo(tetramethylene succinate)-co-(tetramethylane carbonate)] (PBS/C), and poly(epsilon-caprolactone) (PCL). alpha-Chymotrypsin could degrade PLA and PEA with a lower activity on PBS/A. Proteinase K and subtilisin degraded almost all substrates other than PHB. Trypsin and elastase had similar substrate specificities to alpha-chymotrypsin.

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Year:  2005        PMID： 15928850     DOI： 10.1007/s10529-005-2217-8

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN： 0141-5492            Impact factor:   2.461


  10 in total

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