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Use of ultrasonic and pepsin treatment in tandem for collagen extraction from meat industry by‐products
Author(s) -
Ran XueGuang,
Wang LingYun
Publication year - 2014
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.6299
Subject(s) - pepsin , acetic acid , extraction (chemistry) , chromatography , chemistry , denaturation (fissile materials) , biochemistry , solubility , ultrasonic sensor , tendon , enzyme , food science , anatomy , biology , organic chemistry , medicine , nuclear chemistry , radiology
BACKGROUND Relatively little attention is paid to collagen‐rich cattle short tendons (musculus extensor communis, musculus flexor digitorum, musculus digitorum profundis) as a source of high content and relatively pure collagen, a meat‐processing by‐product that is used to a minimal extent. Thus, suitable extraction processes from a meat production by‐product to gain intact collagen is promising, which thus become interesting from an economic and environmental point of view.RESULTS Two extraction methods were compared: a 48 h pepsin treatment using 0.5 mol L −1 acetic acid and an extraction using pepsin treatment after ultrasonic treatment in a 0.5 mol L −1 acetic acid solution (the total ultrasonic and pepsin treatment time was 48 h). The results indicated that the optimal conditions for the extraction of collagen from cattle tendon with the ultrasonic–pepsin tandem method is: 4°C, tendon pre‐swollen for 12 h in 0.5 mol L −1 acetic acid, pepsin amount: 50 U mg −1 of sample, ultrasonic–pepsin tandem treatment time for 18 h and 30 h, respectively. Extracted cattle tendon collagen using ultrasonic and pepsin treatment in tandem was characterised by amino acid analysis, SDS‐PAGE , FT‐IR , solubility and thermal denaturation temperature. The results show that the ultrasonic–pepsin tandem method can effectively improve the efficiency of pepsin extraction of natural collagen without any compromise of the resultant collagen quality.CONCLUSION This study provides a favourable process to deal with poorly extractable residue by use of ultrasonic and pepsin treatment in tandem. Extracted collagen possesses an intact molecular structure, which is useful and particularly important for its biomedical applications, such as drug delivery systems, wound dressings, and scaffolds. © 2013 Society of Chemical Industry