{"title":"工业生产的菜籽粕作为食品工业蛋白质源的生化特性研究","authors":"Petya Ivanova , Vesela Chalova , Galina Uzunova , Lidia Koleva , Ivan Manolov","doi":"10.1016/j.aaspro.2016.09.009","DOIUrl":null,"url":null,"abstract":"<div><p>Rapeseed meal is a by-product of oil production which is primarily used in feed industry. The application of the rapeseed meal as a protein source in food industry is an alternative which leads to a better and more complete use of this by-product. Biochemical characteristics of industrially produced rapeseed meal vary and therefore, detailed analyses prior to its use as a protein source is necessary. The commercial rapeseed meal evaluated in this study contained high protein amount (39.86%) and low residual total fats (2.30%). It was characterized with low levels of glucosinolates (12.69 ± 0.18<!--> <!-->μmol/g) and phenols (1.13 ± 0.04%). Amino acid analysis revealed lysine as the first limiting amino acid with an amino acid score of 58.00%, followed by valine (66.86%). However, this by-product was rich in leucine and isoleucine which amino acid scores equaled to 97.60 and 88.67% respectively. The amino acid score evaluation demonstrated relatively high amount of sulphur containing amino acids (82.57%). The commercial rapeseed meal exhibited low <em>in vitro</em> digestibility (18.59 ± 0.98%). The albumin, globulin and glutelin fractions however, expressed higher digestibility with albumin fraction being the most susceptible (67.22 ± 1.28%) to pepsin and pancreatin proteolytic activities.</p></div>","PeriodicalId":100063,"journal":{"name":"Agriculture and Agricultural Science Procedia","volume":"10 ","pages":"Pages 55-62"},"PeriodicalIF":0.0000,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.aaspro.2016.09.009","citationCount":"29","resultStr":"{\"title\":\"Biochemical Characterization of Industrially Produced Rapeseed Meal as a Protein Source in Food Industry\",\"authors\":\"Petya Ivanova , Vesela Chalova , Galina Uzunova , Lidia Koleva , Ivan Manolov\",\"doi\":\"10.1016/j.aaspro.2016.09.009\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Rapeseed meal is a by-product of oil production which is primarily used in feed industry. The application of the rapeseed meal as a protein source in food industry is an alternative which leads to a better and more complete use of this by-product. Biochemical characteristics of industrially produced rapeseed meal vary and therefore, detailed analyses prior to its use as a protein source is necessary. The commercial rapeseed meal evaluated in this study contained high protein amount (39.86%) and low residual total fats (2.30%). It was characterized with low levels of glucosinolates (12.69 ± 0.18<!--> <!-->μmol/g) and phenols (1.13 ± 0.04%). Amino acid analysis revealed lysine as the first limiting amino acid with an amino acid score of 58.00%, followed by valine (66.86%). However, this by-product was rich in leucine and isoleucine which amino acid scores equaled to 97.60 and 88.67% respectively. The amino acid score evaluation demonstrated relatively high amount of sulphur containing amino acids (82.57%). The commercial rapeseed meal exhibited low <em>in vitro</em> digestibility (18.59 ± 0.98%). The albumin, globulin and glutelin fractions however, expressed higher digestibility with albumin fraction being the most susceptible (67.22 ± 1.28%) to pepsin and pancreatin proteolytic activities.</p></div>\",\"PeriodicalId\":100063,\"journal\":{\"name\":\"Agriculture and Agricultural Science Procedia\",\"volume\":\"10 \",\"pages\":\"Pages 55-62\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2016-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.aaspro.2016.09.009\",\"citationCount\":\"29\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Agriculture and Agricultural Science Procedia\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2210784316302029\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Agriculture and Agricultural Science Procedia","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2210784316302029","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Biochemical Characterization of Industrially Produced Rapeseed Meal as a Protein Source in Food Industry
Rapeseed meal is a by-product of oil production which is primarily used in feed industry. The application of the rapeseed meal as a protein source in food industry is an alternative which leads to a better and more complete use of this by-product. Biochemical characteristics of industrially produced rapeseed meal vary and therefore, detailed analyses prior to its use as a protein source is necessary. The commercial rapeseed meal evaluated in this study contained high protein amount (39.86%) and low residual total fats (2.30%). It was characterized with low levels of glucosinolates (12.69 ± 0.18 μmol/g) and phenols (1.13 ± 0.04%). Amino acid analysis revealed lysine as the first limiting amino acid with an amino acid score of 58.00%, followed by valine (66.86%). However, this by-product was rich in leucine and isoleucine which amino acid scores equaled to 97.60 and 88.67% respectively. The amino acid score evaluation demonstrated relatively high amount of sulphur containing amino acids (82.57%). The commercial rapeseed meal exhibited low in vitro digestibility (18.59 ± 0.98%). The albumin, globulin and glutelin fractions however, expressed higher digestibility with albumin fraction being the most susceptible (67.22 ± 1.28%) to pepsin and pancreatin proteolytic activities.