Preparation and Purification of Recombinant Dipeptidyl Peptidase 4 from Tenebrio molitor

Autor:	Elena N. Elpidina, S. V. Benevolensky, I. Yu. Filippova, E. V. Klyachko, Valeriia F. Tereshchenkova, Ya. E. Dunaevsky, Mikhail A. Belozersky
Rok vydání:	2019
Předmět:	chemistry.chemical_classification medicine.diagnostic_test biology Imino acid Proteolysis biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Dipeptidyl peptidase law.invention Pichia pastoris Enzyme chemistry law Recombinant DNA medicine Storage protein Dipeptidyl peptidase-4
Zdroj:	Applied Biochemistry and Microbiology. 55:218-223
ISSN:	1608-3024 0003-6838
Popis:	Dipeptidyl peptidase 4—is a unique proline-specific peptidase, capable to hydrolyze the bonds, formed by proline amino acid residue, cleaving dipeptides from N-terminus of peptides and proteins, containing this imino acid in P1 position. Recombinant dipeptidyl peptidase 4 from the insect Tenebrio molitor was prepared for the first time in the Pichia pastoris protein expression system; a method for its purification was proposed. The authenticity of the obtained recombinant enzyme was confirmed by mass spectrometry. The use of the obtained preparation of the T. molitor enzyme is promising for the hydrolysis of resistant to proteolysis proline-rich peptides and proteins, particularly for prolamins – the main storage proteins of cereal seeds, since they are not fully hydrolyzed by human digestive enzymes and cause autoimmune gastrointestinal celiac disease in the susceptible group of people.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::b8917c5784ebcc88bd273dcc48dc885b https://doi.org/10.1134/s0003683819030141 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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