Abstract
Bioactive peptides were successfully produced from fish (Gadidae) and beef skeletal muscles after being hydrolyzed for 8 h with pepsin. Subsequently, they were purified using a Sep-Pak C18 cartridge and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weights of pure fish and beef peptides were determined to be 2364.4 and 3771.8, respectively. According to Edman degradation, the fish peptide was composed of 21 amino acid residues (F21), while the beef peptide was composed of 34 amino acid residues (B34). F21 and B34 displayed angiotensin-converting enzyme inhibitory activity with a half maximal inhibitory concentration (IC50) values of 7.3 µg/mL and 5.8 µg/mL, respectively. F21 exhibited antioxidant activity with an IC50 value of 389.9 µg/mL, whereas B34 exhibited no antioxidant activity. Moreover, F21 and B34 displayed antimicrobial effects against a wide spectrum of food-borne pathogens and spoilage bacteria. Bioactive peptides derived from muscle proteins are a promising strategy for the production of functional food materials and safe food preservatives.
Highlights
The aim of this study is to identify bioactive peptides in beef and fish hydrolysates digested with pepsin, as well as evaluate their antimicrobial, antioxidant, and angiotensin-converting enzyme (ACE) inhibitory properties
The fish and beef hydrolysates were purified by means of a Sep-Pak C18 cartridge with
All reversed-phase high-performance liquid chromatography (RP-highperformance liquid chromatography (HPLC)) fractions of fish and beef were analyzed by mass spectrometry, and the purest fractions from fish and beef peptides were selected based on clearance of the mass spectra for further study
Summary
Meat proteins are essential food constituents with nutritional and physiological properties. They are rich in essential amino acids, which are required for development of the body as well as the chemical and sensory characteristics of protein-enclosing products. Meat proteins contain bioactive peptides, which are protein fragments containing certain amino acids. Bioactive peptides are inert in the original protein chains but can be generated by proteolytic digestion. They could pass through the intestine and into the circulation, where they can perform a variety of biological functions. Antimicrobial, angiotensin-converting enzyme (ACE) inhibitory, and antioxidant characteristics have already been reported in a variety of bioactive peptides [2]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
