| Title : Different enantioselectivity of two types of poly(lactic acid) depolymerases toward poly(l-lactic acid) and poly(d-lactic acid) - Kawai_2011_Polym.Degrad.Stab_96_1342 |
| Author(s) : Kawai F , Nakadai K , Nishioka E , Nakajima H , Ohara H , Masaki K , Iefuji H |
| Ref : Polymer Degradation and Stability , 96 :1342 , 2011 |
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Abstract :
Poly(lactic acid) (PLA) depolymerases are categorized into protease-type and lipase-type. Protease-types can hydrolyze poly(L-lactic acid) (PLLA) but not poly(D-lactic acid) (PDLA). Lipase-types, including cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2 preferentially hydrolyze PDLA. Both enzymes degraded not only PLA emulsion but also PLA film, in which amorphous region is preferentially attacked, but crystalline region can be also attacked. Stereocomplex PLA (sc-PLA) formed by 50:50 blending of PLLA and PDLA included no homo crystals, but a tiny homo crystallization peak appeared and crystallinity increased by 5% when attacked by CLE, although no significant change of molecular weight and crystalline size was found. Enantioselective degradation must occur in amorphous region of PLLA/PDLA film and preferentially hydrolyzed PDLA, resulting in a slightly excess amount of PLLA remained, which must be crystallized |
| PubMedSearch : Kawai_2011_Polym.Degrad.Stab_96_1342 |
| PubMedID: |
| Gene_locus related to this paper: crysp-Q874E9 |
| Substrate | Polylactic-acid |
| Gene_locus | crysp-Q874E9 |
Kawai F, Nakadai K, Nishioka E, Nakajima H, Ohara H, Masaki K, Iefuji H (2011)
Different enantioselectivity of two types of poly(lactic acid) depolymerases toward poly(l-lactic acid) and poly(d-lactic acid)
Polymer Degradation and Stability
96 :1342
Kawai F, Nakadai K, Nishioka E, Nakajima H, Ohara H, Masaki K, Iefuji H (2011)
Polymer Degradation and Stability
96 :1342