Your browser doesn't support javascript.
loading
Detoxifying Cyanides Using Cyanase Enzyme Complexes Composed of Carbonic Anhydrase via Irreversible Covalent Bonds.
Sun, Habin; Lee, YouKyeong; Han, Sung Ok; Hyeon, Jeong Eun.
Afiliação
  • Sun H; Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea.
  • Lee Y; Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea.
  • Han SO; Department of Biotechnology, Korea University, Seoul 02841, Republic of Korea.
  • Hyeon JE; Department of Next Generation Applied Sciences, Graduate School, Sungshin Women's University, Seoul 01133, Republic of Korea.
J Agric Food Chem ; 72(10): 5318-5324, 2024 Mar 13.
Article em En | MEDLINE | ID: mdl-38477042
ABSTRACT
Cyanase is a possible solution to reduce the environmental impact of cyanide. However, the enzyme's dependence on HCO3- limits its industrial applications. To overcome this problem, carbonic anhydrase is utilized in this study. Three types of Catcher/Tag systems were introduced into the cyanase (psCYN) from Pseudomonas stutzeri and the carbonic anhydrase (hmCA) from Hydrogenovibrio marinus to construct enzyme complexes via irreversible covalent bonds. Initially, a cyanase complex with the aid of scaffolding proteins was designed. The results of cyanase complexes using scaffolding proteins were similar to or inferior to those of the two free enzymes. To address this, the two enzymes were manipulated to form a direct bioconjugation without the need for scaffolding proteins. The two enzymes forming a direct conjugation showed activity more than 2.5 times higher than that of cyanase alone. In conclusion, this outcome will contribute to solving problems related to residual cyanides in food and the environment.
Assuntos
Palavras-chave

Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Anidrases Carbônicas Idioma: En Revista: J Agric Food Chem Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Anidrases Carbônicas Idioma: En Revista: J Agric Food Chem Ano de publicação: 2024 Tipo de documento: Article