Abstract
Every year, the poultry industry produces a large number of by-products such as chicken heads containing a considerable proportion of proteins, particularly collagen. To prepare gelatin is one of the possibilities to advantageously utilize these by-products as raw materials. The aim of the paper was to process chicken heads into gelatins. An innovative method for conditioning starting raw material was using the proteolytic enzyme. Three technological factors influencing the yield and properties of extracted gelatins were monitored including the amount of enzyme used in the conditioning of the raw material (0.4% and 1.6%), the time of the conditioning (18 and 48 h), and the first gelatin extraction time (1 and 4 h). The gelatin yield was between 20% and 36%. The gelatin gel strength ranged from 113 to 355 Bloom. The viscosity of the gelatin solution was determined between 1.4 and 9.5 mPa.s. The content of inorganic solids varied from 2.3% to 3.9% and the melting point of the gelatin gel was recorded between 34.5 and 42.2 °C. This study has shown that gelatin obtained from chicken heads has a promising potential with diverse possible applications in the food industry, pharmacy, and cosmetics.
Highlights
Gelatin is a partial hydrolysate of collagen, which is a high molecular weight polypeptide
The gel strength decreased with rising values of all studied factors. These results suggest that the reduction in the gel strength likely stems from the disruption of the primary structure in collagen molecules during the enzyme conditioning of the raw material and the gelatin extraction as well
This study investigates the possibilities of the preparation of gelatin from an alternative raw material of chicken heads
Summary
Gelatin is a partial hydrolysate of collagen, which is a high molecular weight polypeptide. It is a water soluble, digestible protein composed of 18 amino acids containing all essential amino acids except for tryptophan [1]. Gelatin is a common raw material in the food industry due to its beneficial characteristics such as gel formation, thickening, clarifying, and stabilizing properties [2,3]. It is formed by denaturation of collagen at temperatures above 60 ◦ C, which causes structural changes, intra-molecular bond breaks, and consequent physical-chemical changes. Chosen method for the production defines the Molecules 2020, 25, 494; doi:10.3390/molecules25030494 www.mdpi.com/journal/molecules
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