Biotechnology Letters

, Volume 27, Issue 7, pp 459–464 | Cite as

Hydrolysis of polyesters by serine proteases

  • Hyun-A Lim
  • Takao Raku
  • Yutaka Tokiwa


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.


biodegradable α-chymotrypsin polyesters poly(L-lactide) serine proteases 


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Copyright information

© Springer 2005

Authors and Affiliations

  1. 1.Institute of Agricultural Science & TechnologyChonbuk National UniversityJeonjuKorea
  2. 2.National Institute of Advanced Industrial Science and Technology (AIST)TsukubaJapan

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