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Hydrolysis of polyesters by serine proteases
Authors:Hyun-A?Lim,Takao?Raku,Yutaka?Tokiwa  author-information"  >  author-information__contact u-icon-before"  >  mailto:y.tokiwa@aist.go.jp"   title="  y.tokiwa@aist.go.jp"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(1) Institute of Agricultural Science & Technology, Chonbuk National University, Jeonju, 561-756, Korea;(2) National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, 1-1-1 Higashi, Tsukuba Ibaraki, 305-8566, Japan
Abstract:The substrate specificity of agr-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(epsiv-caprolactone) (PCL). agr-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 agr-chymotrypsin.
Keywords:biodegradable    /content/kg66867135w35552/xxlarge945.gif"   alt="  agr"   align="  BASELINE"   BORDER="  0"  >-chymotrypsin  polyesters  poly(  font-variant:small-caps"  >L-lactide)  serine proteases
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