Zobrazeno 1 - 10
of 173
pro vyhledávání: '"Fusako Kawai"'
Autor:
Saroya Bilraheem, Sirasit Srinuanpan, Benjamas Cheirsilp, Apichat Upaichit, Fusako Kawai, Uschara Thumarat
Publikováno v:
Foods, Vol 13, Iss 16, p 2554 (2024)
Food wastes have a large number of functional ingredients that have potential for valorization. Melon peels are increasingly produced as waste in food industries in Thailand. This study aimed to optimize pectin extraction conditions from melon peel f
Externí odkaz:
https://doaj.org/article/0e7e2ce1db0a464899a3018f3048fb32
Autor:
Fusako Kawai, Yoshitomo Furushima, Norihiro Mochizuki, Naoki Muraki, Mitsuaki Yamashita, Akira Iida, Rie Mamoto, Takehiko Tosha, Ryo Iizuka, Sakihito Kitajima
Publikováno v:
AMB Express, Vol 12, Iss 1, Pp 1-15 (2022)
Key points 1. The increased surface area of PET promotes its hydrolysis by Cut190, supporting the surface erosion mechanism by a two-step process (endo-type scission of a polymer chain and exo-type hydrolysis of depolymerized fragments). 2. Dodecyltr
Externí odkaz:
https://doaj.org/article/56c59646bf7e47f89ef12bceb0ee1978
Autor:
Fusako Kawai
Publikováno v:
Catalysts, Vol 11, Iss 2, p 206 (2021)
This short paper reviews two groups of enzymes designated as polyethylene terephthalate (PET) hydrolases: one consists of thermophilic cutinases from thermophilic microorganisms (actinomycetes and a fungus) and the other consists of mesophilic cutina
Externí odkaz:
https://doaj.org/article/a6677ce85e934aeb8cb86a0b2ed18886
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 6, Pp 13579-13594 (2015)
A thermostable esterase gene (hydS14) was cloned from an Actinomadura sp. S14 gene library. The gene is 777 bp in length and encodes a polypeptide of 258 amino acid residues with no signal peptide, no N-glycosylation site and a predicted molecular ma
Externí odkaz:
https://doaj.org/article/b3427009ed8e422e971f2c316632e48a
Publikováno v:
International Journal of Molecular Sciences, Vol 14, Iss 1, Pp 1218-1231 (2013)
Ethoxy (EO) chain nonylphenol dehydrogenase (NPEO-DH) from Ensifer sp. AS08 and EO chain octylphenol dehydrogenase from Pseudomonas putida share common molecular characteristics with polyethylene glycol (PEG) dehydrogenases (PEG-DH) and comprise a PE
Externí odkaz:
https://doaj.org/article/b2e6ba15f0ae42ffb471b7d1bf3b769c
Autor:
Fusako Kawai
Publikováno v:
ChemSusChem. 14:4115-4122
The research on polyethylene terephthalate (PET) hydrolyzing enzymes started in 2005; several studies are now nearing the objective of their application in biorecycling of PET, which is an urgent environmental issue. The thermostability of PET hydrol
Autor:
Fusako Kawai, Masaji Watanabe
Publikováno v:
Journal of Materials Science and Chemical Engineering. :43-50
This study demonstrates mathematical analysis of biodegradation processes of xenobiotic polymers. A model for microbial population is based on the fact that growth rate of microorganisms is proportional to the microbial population and consumption rat
Autor:
Narutoshi Kamiya, Nobutaka Numoto, Masayuki Oda, Miho Emori, Akane Senga, Nobutoshi Ito, Fusako Kawai, Yuma Kobayashi, Gert-Jan Bekker
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 89:502-511
The cutinase-like enzyme from the thermophile Saccharomonospora viridis AHK190, Cut190, is a good candidate to depolymerize polyethylene terephthalate (PET) efficiently. We previously developed a mutant of Cut190 (S226P/R228S), which we designated as
Autor:
Fusako Kawai
Publikováno v:
KAGAKU TO SEIBUTSU. 58:362-368
Publikováno v:
ACS Sustainable Chemistry & Engineering. 8:8894-8908
Polyethylene terephthalate (PET) hydrolase is a challenging target as PET is a commonly used plastic that is extremely resistant to enzymatic attack. Since the discovery of a PET hydrolase from The...