Functional and bioactive properties of collagen and gelatin from alternative sources: A review

• Published in: Food hydrocolloids 2011-12, Vol.25 (8), p.1813-1827
• Main Authors: Gómez-Guillén, M.C., Giménez, B., López-Caballero, M.E., Montero, M.P.
• Format: Article
• Language: English
• Subjects: Animal productions; Bioactive peptides; Biological and medical sciences; Byproducts; Collagen; Collagens; Cosmetics; Fish; Foaming agents; Food additives; Food industries; Foods; Functional properties; Fundamental and applied biological sciences. Psychology; Gelatin; Gelatins; General aspects; Hydrolysis; Peptides; Poultry; Terrestrial animal productions; Vertebrates
• ISSN: 0268-005X; 1873-7137
• DOI: 10.1016/j.foodhyd.2011.02.007

The rising interest in the valorisation of industrial by-products is one of the main reasons why exploring different species and optimizing the extracting conditions of collagen and gelatin has attracted the attention of researchers in the last decade. The most abundant sources of gelatin are pig skin, bovine hide and, pork and cattle bones, however, the industrial use of collagen or gelatin obtained from non-mammalian species is growing in importance. The classical food, photographic, cosmetic and pharmaceutical application of gelatin is based mainly on its gel-forming properties. Recently, and especially in the food industry, an increasing number of new applications have been found for gelatin in products such as emulsifiers, foaming agents, colloid stabilizers, biodegradable film-forming materials and micro-encapsulating agents, in line with the growing trend to replace synthetic agents with more natural ones. In the last decade, a large number of studies have dealt with the enzymatic hydrolysis of collagen or gelatin for the production of bioactive peptides. Besides exploring diverse types of bioactivities, of an antimicrobial, antioxidant or antihypertensive nature, studies have also focused on the effect of oral intake in both animal and human models, revealing the excellent absorption and metabolism of Hyp-containing peptides. The present work is a compilation of recent information on collagen and gelatin extraction from new sources, as well as new processing conditions and potential novel or improved applications, many of which are largely based on induced cross-linking, blending with other biopolymers or enzymatic hydrolysis. [Display omitted]