Acetylcholinesterase-inhibitor hydrolysates obtained from ‘in vitro’ enzymatic hydrolysis of mannoproteins extracted from different strains of yeasts
Autor: | Arturo Carlos Simonetta, Silvina R. Drago, Roque Spinelli, Pablo Gabriel Spontón, Georgina Tonarelli |
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Rok vydání: | 2015 |
Předmět: |
01 natural sciences
Saccharomyces FUNCTIONAL FOOD Industrial and Manufacturing Engineering Hydrolysate ACETYLCHOLINESTERASE Enzymatic hydrolysis Pichia Chymotrypsin Chromatography biology 010405 organic chemistry Otras Ciencias Químicas 010401 analytical chemistry YEASTS Ciencias Químicas Proteolytic enzymes BIOACTIVE PEPTIDES biology.organism_classification Proteinase K Yeast 0104 chemical sciences Biochemistry biology.protein MANNOPROTEINS CIENCIAS NATURALES Y EXACTAS Food Science |
Zdroj: | International Journal of Food Science & Technology. 51:300-308 |
ISSN: | 0950-5423 |
DOI: | 10.1111/ijfs.12940 |
Popis: | In vitro inhibitory activity against acetylcholinesterase (AChE) of peptides obtained by enzymatic hydrolysis of mannoproteins extracted from strains of yeasts was investigated. Yeast mannoproteins were extracted from strains belonging to the genera Brettanomyces, Candida, Pichia and Saccharomyces isolated from dairy products. They were obtained by heat treatment in citrate buffer and purified by affinity chromatography with concanavalin A. Each purified extract was subsequently hydrolysed with proteolytic enzymes (trypsin, pepsin, chymotrypsin and proteinase K) applied individually or in combination, thus generating smaller peptides. Inhibitory activity of the latter against AChE was determined. The molecular weight of mannoproteins, determined by SDS-PAGE, was between 6.5 and 30 kDa. As regards AChE inhibition, a preliminary screening of all hydrolysed extracts was performed, yielding variable results with 59% maximum inhibition. Subsequently, when inhibitory concentration 50 (IC50) was determined, the extracts showed higher inhibitory activity (between 6.75 and 12.3 mg mL-1). Results showed that the mannoproteins separated from yeast strains of food origin generated bioactive peptides by enzymatic hydrolysis, which can be of interest to the manufacturing of food with potential functional properties. Different peptide extracts were obtained by enzymatic hydrolysis of yeast mannoproteins and their in vitro inhibitory activity against acetylcholinesterase (AChE) was investigated. The most active extracts showed IC50 between 6.75 and 12.3 mg mL-1. Fil: Spontón, Pablo Gabriel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina Fil: Spinelli, Roque. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica; Argentina Fil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina Fil: Tonarelli, Georgina Guadalupe. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica; Argentina Fil: Simonetta, Arturo Carlos. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina |
Databáze: | OpenAIRE |
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