Preparation of gelatin from broiler chicken stomach collagen

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F70883521%3A28110%2F23%3A63564858" target="_blank" >RIV/70883521:28110/23:63564858 - isvavai.cz</a>

Result on the web

<a href="https://www.mdpi.com/2304-8158/12/1/127" target="_blank" >https://www.mdpi.com/2304-8158/12/1/127</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/foods12010127" target="_blank" >10.3390/foods12010127</a>

Result language

angličtina

Original language name

Preparation of gelatin from broiler chicken stomach collagen

Original language description

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®) 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 °C). Data were statistically processed and analyzed at a significance level of 95%. The gelatin yield averaged 65 ± 8%; the gel strength ranged from 25 ± 1 to 439 ± 6 Bloom, the viscosity from 1.0 ± 0.4 to 3.40 ± 0.03 mPa·s, gelling point from 14.0 ± 2.0 to 22.0 ± 2.0 °C, melting point from 28.0 ± 1.0 to 37.0 ± 1.0 °C. The digestibility of gelatin was 100.0% in all samples; the ash content was very low (0.44 ± 0.02–0.81 ± 0.02%). The optimal conditions for the enzymatic treatment of collagen from chicken stomachs were achieved at a higher temperature (70.0 °C) and a lower amount of enzyme (0.10–0.15%). 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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

21101 - Food and beverages

Project

—

Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2023

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Foods

ISSN

2304-8158

e-ISSN

—

Volume of the periodical

12

Issue of the periodical within the volume

1

Country of publishing house

CH - SWITZERLAND

Number of pages

18

Pages from-to

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UT code for WoS article

000909281300001

EID of the result in the Scopus database

2-s2.0-85145862133