Abstract
The substrate specificity of α-chymotrypsin and other serine proteases, trypsin, elastase, proteinase K and subtilisin, towards hydrolysis of various polyesters was examined using poly(L-lactide) (PLA), poly(β-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(ɛ-caprolactone) (PCL). α-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 α-chymotrypsin.
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Lim, HA., Raku, T. & Tokiwa, Y. Hydrolysis of polyesters by serine proteases. Biotechnol Lett 27, 459–464 (2005). https://doi.org/10.1007/s10529-005-2217-8
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DOI: https://doi.org/10.1007/s10529-005-2217-8