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Carboxymethyl Cellulose-Based Polymers as Promising Matrices for Ficin Immobilization.
Sorokin, Andrey V; Goncharova, Svetlana S; Lavlinskaya, Maria S; Holyavka, Marina G; Faizullin, Dzhigangir A; Kondratyev, Maxim S; Kannykin, Sergey V; Zuev, Yuriy F; Artyukhov, Valeriy G.
Afiliação
  • Sorokin AV; Biophysics and Biotechnology Department, Voronezh State University, 1 Universitetskaya Square, 394018 Voronezh, Russia.
  • Goncharova SS; Laboratory of Bioresource Potential of Coastal Area, Institute for Advanced Studies, Sevastopol State University, 33 Studencheskaya Street, 299053 Sevastopol, Russia.
  • Lavlinskaya MS; Laboratory of Metagenomics and Food Biotechnologies, Voronezh State University of Engineering Technologies, 19 Revolutsii Avenue, 394036 Voronezh, Russia.
  • Holyavka MG; Biophysics and Biotechnology Department, Voronezh State University, 1 Universitetskaya Square, 394018 Voronezh, Russia.
  • Faizullin DA; Biophysics and Biotechnology Department, Voronezh State University, 1 Universitetskaya Square, 394018 Voronezh, Russia.
  • Kondratyev MS; Laboratory of Bioresource Potential of Coastal Area, Institute for Advanced Studies, Sevastopol State University, 33 Studencheskaya Street, 299053 Sevastopol, Russia.
  • Kannykin SV; Laboratory of Metagenomics and Food Biotechnologies, Voronezh State University of Engineering Technologies, 19 Revolutsii Avenue, 394036 Voronezh, Russia.
  • Zuev YF; Biophysics and Biotechnology Department, Voronezh State University, 1 Universitetskaya Square, 394018 Voronezh, Russia.
  • Artyukhov VG; Laboratory of Bioresource Potential of Coastal Area, Institute for Advanced Studies, Sevastopol State University, 33 Studencheskaya Street, 299053 Sevastopol, Russia.
Polymers (Basel) ; 15(3)2023 Jan 27.
Article em En | MEDLINE | ID: mdl-36771951
ABSTRACT
The present work is devoted to research on the interaction between carboxymethyl cellulose sodium salt and its derivatives (graft copolymer of carboxymethyl cellulose sodium salt and N,N-dimethyl aminoethyl methacrylate) with cysteine protease (ficin). The interaction was studied by FTIR and by flexible molecular docking, which have shown the conjugates' formation with both matrices. The proteolytic activity assay performed with azocasein demonstrated that the specific activities of all immobilized ficin samples are higher in comparison with those of the native enzyme. This is due to the modulation of the conformation of ficin globule and of the enzyme active site by weak physical interactions involving catalytically valuable amino acids. The results obtained can extend the practical use of ficin in biomedicine and biotechnology.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2023 Tipo de documento: Article