Journal
MACROMOLECULAR BIOSCIENCE
Volume 16, Issue 1, Pages 151-159Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/mabi.201500255
Keywords
cysteine; oligomerization; peptides; proteinase K; thermostable
Funding
- National Natural Science Foundation of China (NSFC) [51225306]
- RIKEN Biomass Engineering Program
- Impulsing Paradigm Change through Disruptive Technologies Program (ImPACT)
- RIKEN International Program Associate
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Oligomerization of thiol-unprotected L-cysteine ethyl ester (Cys-OEt) catalyzed by proteinase K in aqueous solution has been used to synthesize oligo(L-cysteine) (OligoCys) with a well-defined chemical structure and relatively large degree of polymerization (DP) up to 16-17 (average 8.8). By using a high concentration of Cys-OEt, 78.0% free thiol content was achieved. The thermal properties of OligoCys are stable, with no glass transition until 200 degrees C, and the decomposition temperature could be increased by oxidation. Chemoenzymatically synthesized OligoCys has great potential for use as a thermostable bio-based material with resistance to oxidation.
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