Use of a Commercial Protease and Yeasts To Obtain CGRP-like Molecules from Saithe Protein

• Published in: Journal of agricultural and food chemistry Vol. 56; no. 17; pp. 7853 - 7859
• Main Authors: Martínez-Alvarez, Oscar, Guimas, Laurence, Delannoy, Charles, Fouchereau-Peron, Martine
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 10.09.2008
• Subjects: Animals; Bioactive Constituents; bioactive properties; Biological and medical sciences; calcitonin; calcitonin gene-related peptide; Calcitonin Gene-Related Peptide - chemistry; Calcitonin Gene-Related Peptide - isolation & purification; CGRP; Chromatography, High Pressure Liquid; filleting; fish protein hydrolysate; Fish Proteins - chemistry; Fish Proteins - metabolism; Food industries; Functional foods; Fundamental and applied biological sciences. Psychology; Gadiformes; Peptide Hydrolases - metabolism; Pollachius virens; protein hydrolysate; proteinases; Radioligand Assay; Saccharomyces cerevisiae; Saccharomyces cerevisiae - metabolism; saithe; Sequence Analysis, Protein; Subtilisins - metabolism; yeasts; saithe; Functional foods; CGRP; Saccharomyces cerevisiae; protein hydrolysate; Pollachius virens; Ascomycota; Yeast; Enzyme; Commercial use; Protein; Fungi; Peptidases; Vertebrata; Health food; Hydrolysate; Pisces; Hydrolases
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf801393r

Different bioactive molecules, such as CGRP-like peptides, can be found in fish protein hydrolysates. Calcitonin gene-related peptide (CGRP) is a neuropeptide known to act as a potent arterial and venous vasodilator in humans. This study focuses on the industrial obtaining of CGRP-like molecules from saithe (Pollachius virens) byproduct, derived from the filleting process. Protein from P. virens was primarily hydrolyzed with Alcalase and later treated with Saccharomyces cerevisiae live cells. Treatment with Saccharomyces doubled the quantity of bioactive molecules obtained. The CGRP-like molecules were partially purified by chromatography, and the immunoreactive material was further analyzed for its CGRP-like bioactivity, using a specific radioreceptor assay. The concentration of CGRP-like molecules increased over 100-fold after purification. The bioactive molecules were able to induce cyclic AMP stimulation in rat liver membranes. Finally, partial sequencing of the bioactive peptide was performed, showing some homology with α-actin and myosin of several fish species.