Preparation of Gelatin from Broiler Chicken Stomach Collagen

With the increasing consumption of poultry meat around the world, the use of chicken stomachs as a source of collagen is being offered. The objective of this study was to extract gelatin from the stomachs of broiler chickens and to estimate their gel strength, ash content, viscosity, gelling point, melting point, clarity and digestibility. An innovative biotechnological method based on the conditioning of collagen with a microbial endoproteinase (Protamex&reg:) and hot-water extraction was used to control the chemical and thermal denaturation process of collagen to prepare gelatin. The experiments were planned using a Taguchi design, 2 factors at 3 levels: factor A for the amount of proteolytic enzyme (0.10, 0.15 and 0.20%) and factor B for the extraction temperature (55.0, 62.5 and 70.0 &deg:C). Data were statistically processed and analyzed at a significance level of 95%. The gelatin yield averaged 65 &plusmn: 8%: the gel strength ranged from 25 &plusmn: 1 to 439 &plusmn: 6 Bloom, the viscosity from 1.0 &plusmn: 0.4 to 3.40 &plusmn: 0.03 mPa&middot:s, gelling point from 14.0 &plusmn: 2.0 to 22.0 &plusmn: 2.0 &deg:C, melting point from 28.0 &plusmn: 1.0 to 37.0 &plusmn: 1.0 &deg:C. The digestibility of gelatin was 100.0% in all samples: the ash content was very low (0.44 &plusmn: 0.02&ndash:0.81 &plusmn: 0.02%). The optimal conditions for the enzymatic treatment of collagen from chicken stomachs were achieved at a higher temperature (70.0 &deg:C) and a lower amount of enzyme (0.10&ndash:0.15%). Conditioning chicken collagen with a microbial endoproteinase is an economically and environmentally friendly processing method, an alternative to the usual acid- or alkaline-based treatment that is used industrially. The extracted products can be used for food and pharmaceutical applications.