{"title":"Rooster Collagen Extracts from Rooster by-Products","authors":"K. A. Munasinghe, J. Schwarz","doi":"10.15406/JNHFE.2017.07.00239","DOIUrl":null,"url":null,"abstract":"Collagen associated hydrolysates have desirable characteristics for various industrial applications [1,2]. They have been used as important biomaterial in medical applications because of their biodegradability and weak antigenicity [3]. In addition, intracellular and extra-cellular self-assembly of polypeptide chains and the cross-links between adjacent molecules help collagen fibrils to withstand physical stress [4]. Collagen is also effective in decreasing cooking loss of deli products containing chunked chicken meat by increasing protein-protein bindings, and has the potential to improve the quality characteristics of deli rolls by improving their texture [5]. Further, Mittal [6] showed that collagen hydrolysates can be used as binders or extenders in meat emulsions. Moreover, collagen can also be used to make natural casings for sausages and frankfurters [7] and to fill periodontal bony pockets [8]. Collagen is however, deficient in the essential amino acid tryptophan and limited in some essential amino acids such as lysine, threonine and methionine [9].","PeriodicalId":331573,"journal":{"name":"Journal of Nutritional Health & Food Engineering","volume":"7 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2017-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Nutritional Health & Food Engineering","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15406/JNHFE.2017.07.00239","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
Collagen associated hydrolysates have desirable characteristics for various industrial applications [1,2]. They have been used as important biomaterial in medical applications because of their biodegradability and weak antigenicity [3]. In addition, intracellular and extra-cellular self-assembly of polypeptide chains and the cross-links between adjacent molecules help collagen fibrils to withstand physical stress [4]. Collagen is also effective in decreasing cooking loss of deli products containing chunked chicken meat by increasing protein-protein bindings, and has the potential to improve the quality characteristics of deli rolls by improving their texture [5]. Further, Mittal [6] showed that collagen hydrolysates can be used as binders or extenders in meat emulsions. Moreover, collagen can also be used to make natural casings for sausages and frankfurters [7] and to fill periodontal bony pockets [8]. Collagen is however, deficient in the essential amino acid tryptophan and limited in some essential amino acids such as lysine, threonine and methionine [9].