Collagen production from chicken keel bone using acid and enzymatic treatment at a temperature of 30 °C

Abstract

The aim of this study was to investigate the effect of acid pretreatment, temperature and enzyme concentration on the acid-enzymatic extraction of soluble collagen from chicken keel bone cartilage. A chemical composition analysis and protein profile characterization of this slaughter by-product were also conducted. The cartilages were extracted with 0.5 mol/L of acetic, lactic and citric acids for 24, 48 and 72 hours. Subsequently, optimization with a 2 2 factorial design was performed with three replications at the central point for a total of 7 experiments; the analyzed response was the collagen content of the obtained isolates. The cartilage under study has a high protein content (90.27% dry basis) consisting of approximately 35.7% collagen and is a source of essential and predominantly hydrophobic amino acids. Pretreatment with acetic acid for 24 hours led to greater extraction potential and consequently, a better collagen yield (30.12%). The electrophoretic profile of the obtained collagens revealed the existence of an α1 chain, indicating that this collagen was type OO. Statistical analysis demonstrated that the acid-enzymatic procedure favored a temperature of 30 °C.

Functional properties and antioxidant activity of gelatine and hydrolysate from deer antler base

“…Gel permeation chromatography provides information regarding the Mw and molecular weight distribution of deer antler base gelatine as shown in acids before and after hydrolysis and are classified as umami amino acids. This result was consistent with those for gelatine from bones, such as chicken keel bone (Cordeiro et al, 2020) and skipjack tuna bone (Yang, Zhao, Qiu, Chi, & Wang, 2019). Some amino acids, such as aspartic acid, serine, and glutamic acid, were sensitive to hydrolysis and showed a considerable decrease in concentration.…”

“…Other amino acids, such as cysteine, lysine, histidine, and all the hydrophobic amino acids, controlled the emulsification properties of the emulsified products (Cordeiro et al, 2020).…”

Characteristics of Reconstituted Collagen Fibers from Chicken Keel Cartilage Depends on Salt Type for Removal of Proteoglycans

“…The differences result probably from the age of the chickens (very young 5-week-old broilers were studied, whereas in other studies, the age was over 7 weeks [13]). However, there is no difference in the share of ash per dry matter between our own and other studies [12,14]; this value is low and amounts to about 7%, indicating that the cartilage is not mineralized. In fish and reptile cartilage tissues, the total protein level is higher than in poultry cartilage, ranging from 12% to 15%, which is mainly due to the higher dry matter content of 25-45% [15,16].…”

Collagen Biopolymer in Textile Wet Processing

“…Collagen molecules become more positively charged in acidic environments, and this positive charge helps their solubilization by producing repulsion among tropocollagen molecules. [17] Organic acids, including i) acetic acid (CH3COOH) [20,21], ii) citric acid (C6H8O7) [22], iii) tartaric acid (C4H6O6) and iv) chloroacetic acid and inorganic acids such as i) hydrochloric acid (HCl) and ii) formic acid (CH2O2), are used for the isolation of collagen. [4] Organic acids, on the other hand, are more successful than inorganic acids at cleaving the crosslinks of collagen molecules, resulting in better collagen extractability.…”