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Biodegradable plastic-degrading enzyme from Pseudozyma antarctica: cloning, sequencing, and characterization
Authors:Yukiko Shinozaki  Tomotake Morita  Xiao-hong Cao  Shigenobu Yoshida  Motoo Koitabashi  Takashi Watanabe  Ken Suzuki  Yuka Sameshima-Yamashita  Toshiaki Nakajima-Kambe  Takeshi Fujii  Hiroko K Kitamoto
Institution:1. National Institute for Agro-Environmental Sciences (NIAES), 3-1-3 Kannondai, Tsukuba, Ibaraki, 305-8604, Japan
2. Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5-2, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan
3. Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305-8572, Japan
Abstract:Pseudozyma antarctica JCM 10317 exhibits a strong degradation activity for biodegradable plastics (BPs) such as agricultural mulch films composed of poly(butylene succinate) (PBS) and poly(butylene succinate-co-adipate) (PBSA). An enzyme named PaE was isolated and the gene encoding PaE was cloned from the strain by functional complementation in Saccharomyces cerevisiae. The deduced amino acid sequence of PaE contains 198 amino acids with a predicted molecular weight of 20,362.41. High identity was observed between this sequence and that of cutinase-like enzymes (CLEs) (61–68 %); therefore, the gene encoding PaE was named PaCLE1. The specific activity of PaE against emulsified PBSA was 54.8?±?6.3 U/mg. In addition to emulsified BPs, PaE degraded solid films of PBS, PBSA, poly(ε-caprolactone), and poly(lactic acid).
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