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Switchable CO2-Responsive Janus Nanoparticle for Lipase Catalysis in Pickering Emulsion.
Wang, Wei; Zhou, Ruoyu; Di, Simiao; Mao, Xiangzhao; Huang, Wen-Can.
Afiliação
  • Wang W; State Key Laboratory of Marine Food Processing and Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China.
  • Zhou R; Qingdao Key Laboratory of Food Biotechnology, Qingdao 266404, China.
  • Di S; Key Laboratory of Biological Processing of Aquatic Products, China National Light Industry, Qingdao 266404, China.
  • Mao X; State Key Laboratory of Marine Food Processing and Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China.
  • Huang WC; Qingdao Key Laboratory of Food Biotechnology, Qingdao 266404, China.
J Agric Food Chem ; 72(17): 9967-9973, 2024 May 01.
Article em En | MEDLINE | ID: mdl-38639643
ABSTRACT
The use of convertible immobilized enzyme carriers is crucial for biphasic catalytic reactions conducted in Pickering emulsions. However, the intense mechanical forces during the conversion process lead to enzyme leakage, affecting the stability of the immobilized enzymes. In this study, a CO2-responsive switchable Janus (CrSJ) nanoparticle (NP) was developed using silica NP, with one side featuring aldehyde groups and the other side adsorbing N,N-dimethyldodecylamine. A switchable Pickering emulsion catalytic system for biphasic interface reactions was prepared by covalently immobilizing lipase onto the CrSJ NPs. The CO2-responsive nature of the CrSJ NPs allowed for rapid conversion of the Pickering emulsion, and covalent immobilization substantially reduced lipase leakage while enhancing the stability of the immobilization during the conversion process. Impressively, after repeated transformations, the Pickering emulsion still maintains its original structure. Following 10 consecutive cycles of esterification and hydrolysis reactions, the immobilized enzyme's activity remains at 77.7 and 79.5% of its initial activity, respectively. The Km of the CrSJ catalytic system showed no significant change compared to the free enzyme, while its Vmax values were 1.2 and 1.6 times that of the free enzyme in esterification and hydrolysis reactions, respectively.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dióxido de Carbono / Emulsões / Enzimas Imobilizadas / Nanopartículas / Biocatálise / Lipase Idioma: En Revista: J Agric Food Chem Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Dióxido de Carbono / Emulsões / Enzimas Imobilizadas / Nanopartículas / Biocatálise / Lipase Idioma: En Revista: J Agric Food Chem Ano de publicação: 2024 Tipo de documento: Article