title: Enzymatic hydrolysis of blue whiting (Micromesistius poutassou); functional and bioactive properties.
abstract: Functional and biochemical properties of fish protein hydrolysates (FPH) from blue whiting (BW) were studied. FPH (2.5%, 5%, 10%, and 15% degree of hydrolysis [DH]) were made from isolated proteins from headed and gutted BW with Alcalase 2.4 L. The properties of dried BW mince and protein isolate compared to 4 reference proteins (soy and milk protein) were studied: color, solubility, water-holding capacity (WHC), oil-binding capacity (OBC), emulsion capacity (EC), and emulsion stability (ES). The angiotensin I-converting enzyme (ACE) inhibitory activities of the soluble fraction of BW powders were also investigated. Furthermore, the products were characterized by analyzing their chemical composition. Chemical composition, solubility, OBC, and EC of the BW powders was significantly (P < 0.05) different with different DH, while color, ES, and WHC were not significantly (P > 0.05) different. Salt content of the FPH was high (4% to 19%) and increased with increased DH. Protein solubility varied from 10% to 70% and increased with increased DH. WHC of the FPH was around 97% and was higher than that of all the reference proteins tested. OBC decreased with increased DH (from 3.5 to 2.1 g oil/g protein) and was higher than OBC of the soy and milk proteins (1.6 to 1.9 g oil/g protein). EC of FPH was similar or lower than the reference proteins. ES of FPH (60% to 90%) was similar to or lower than soy and whey proteins (60% to 98%) but higher than casein (20%). ACE inhibition activity increased as DH was increased. Practical Application: The results from this study demonstrate that a functional bioactive hydrolysate can be produced from BW, which is an underutilized fish species, and may aid the industry in better utilizing this raw material. The novelty of this research was the use of BW as a raw material where the protein has been isolated with the pH shift method. Furthermore, it was novel that bioactivity and functionality was measured in the same samples.
authors.affiliation: Matis-Icelandic Food & Biotech R&D, Vinlandsleid 13, 113 Reykjavik, Iceland. mg@matis.is
authors.forename: Margret
authors.initials: M
authors.lastname: Geirsdottir
authors.forename: Sjofn
authors.initials: S
authors.lastname: Sigurgisladottir
authors.forename: Patricia Y
authors.initials: PY
authors.lastname: Hamaguchi
authors.forename: Gudjon
authors.initials: G
authors.lastname: Thorkelsson
authors.forename: Ragnar
authors.initials: R
authors.lastname: Johannsson
authors.forename: Hordur G
authors.initials: HG
authors.lastname: Kristinsson
authors.forename: Magnus M
authors.initials: MM
authors.lastname: Kristjansson
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D000818:Animals; D055598:Chemical Phenomena; D003116:Color; D045703:Emulsifying Agents / Q000737:chemistry* / Q000494:pharmacology; D004655:Emulsions; D029941:Fish Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D005503:Food Additives / Q000737:chemistry* / Q000494:pharmacology; D048388:Gadiformes; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010938:Plant Oils / Q000032:analysis; D011492:Protein Hydrolysates / Q000737:chemistry* / Q000494:pharmacology; D017673:Sodium Chloride, Dietary / Q000032:analysis; D012995:Solubility; D013381:Subtilisins / Q000378:metabolism; D014867:Water / Q000032:analysis
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D045703:Emulsifying Agents; D004655:Emulsions; D029941:Fish Proteins; D005503:Food Additives; D010938:Plant Oils; D011492:Protein Hydrolysates; D017673:Sodium Chloride, Dietary; D014867:Water; D013381:Subtilisins