Structural basis for Ca2+-dependent catalysis of a cutinase-like enzyme and its engineering: application to enzymatic PET depolymerization
Author:
Affiliation:
1. Graduate School of Life and Environmental Sciences, Kyoto Prefectural University
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/18/0/18_bppb-v18.018/_pdf
Reference25 articles.
1. [1] Chen, S., Su, L., Chen, J. & Wu, J. Cutinase: characteristics, preparation, and application. Biotechnol. Adv. 31, 1754–1767 (2013). DOI: 10.1016/j.biotechadv.2013.09.005
2. [2] Kawai, F., Kawabata, T. & Oda, M. Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields. Appl. Microbiol. Biotech. 103, 4253–4268 (2019). DOI: 10.1007/s00253-019-09717-y
3. [3] Zimmermann, W. & Billig, S. Enzymes for the biofunctionalization of poly(ethylene terephthalate). Adv. Biochem. Eng. Biotechnol. 125, 97–120 (2011). DOI: 10.1007/10_2010_87
4. [4] Kawai, F., Kawabata, T. & Oda, M. Current state and perspectives related to the PET hydrolases available for biorecycling. ACS Sustainable Chem. Eng. 8, 8894–8908 (2020). DOI: 10.1021/acssuschemeng.0c01638
5. [5] Kawai, F., Oda, M., Tamashiro, T., Waku, T., Tanaka, N., Yamamoto, M., et al. A novel Ca2+-activated, thermostabilized polyesterase capable of hydrolyzing polyethylene terephthalate from Saccharomonospora viridis AHK190. Appl. Microbiol. Biotechnol. 98, 10053–10064 (2014). DOI: 10.1007/s00253-014-5860-y
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