Non-thermal processing has an impact on the digestibility of the muscle proteins. Issue 28 (3rd October 2022)

• Record Type: Journal Article
• Authors: Bhat, Zuhaib F.; Morton, James D.; Bekhit, Alaa El-Din A.; Kumar, Sunil; Bhat, Hina F.
• Is Part Of: Critical reviews in food science and nutrition. Volume 62:Issue 28(2022)
• Page Start: 7773
• Page End: 7800
• Publication Date: 2022-10-03
• Subjects: Aging -- comminution -- curing -- drying -- gastrointestinal digestion -- in vivo and in vitro studies -- marination -- mechanisms -- muscle composition and fiber type -- muscle proteins -- protein digestibility -- ripening; Food industry and trade -- Periodicals; Nutrition -- Periodicals; Nutrition -- Periodicals; Food -- Periodicals; Diet -- Periodicals; Review Literature -- Periodicals; Nutrition; Food; Diet; Review Literature; 664
• DOI: 10.1080/10408398.2021.1918629
• Languages: English
• ISSNs: 1040-8398

Abstract

Abstract: Muscle proteins undergo several processes before being ready in a final consumable form. All these processes affect the digestibility of muscle proteins and subsequent release of amino acids and peptides during digestion in the human gut. The present review examines the effects of different processing techniques, such as curing, drying, ripening, comminution, aging, and marination on the digestibility of muscle proteins. The review also examines how the source of muscle proteins alters the gastrointestinal protein digestion. Processing techniques affect the structural and functional properties of muscle proteins and can affect their digestibility negatively or positively depending on the processing conditions. Some of these techniques, such as aging and mincing, can induce favorable changes in muscle proteins, such as partial unfolding or exposure of cleavage sites, and increase susceptibility to hydrolysis by digestive enzymes whereas others, such as drying and marination, can induce unfavorable changes, such as severe cross-linking, protein aggregation, oxidation induced changes or increased disulfide (S-S) bond content, thereby decreasing proteolysis. The underlying mechanisms have been discussed in detail and the conclusions drawn in the light of existing knowledge provide information with potential industrial importance.