Determination of the myofibrillar and connective tissue protein contents and amino acid composition of selected composite meat products

1988 ◽  
Vol 36 (6) ◽  
pp. 1109-1121 ◽  
Author(s):  
Constantinos N. Karatzas ◽  
Constantinos G. Zarkadas
1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall

1. Guinea-pig caseins A, B and C were purified free of each other by a combination of ion-exchange chromatography and gel filtration. 2. Determination of the amino acid composition showed all three caseins to contain a high proportion of proline and glutamic acid, but no cysteine. This apart, the amino acid composition of the three caseins was markedly different, though calculated divergence values suggest that some homology may exist between caseins A and B. Molecular-weight estimates based on amino acid composition were in good agreement with those based on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. N-Terminal analysis showed lysine, methionine and lysine to be the N-terminal residues of caseins A, B and C respectively. 4. Two-dimensional separation of tryptic digests revealed a distinctive pattern for each casein. 5. All caseins were shown to be phosphoproteins. The casein C preparation also contained significant amounts of sialic acid, neutral and amino sugars. 6. The results suggest that each casein represents a separate gene product, and that the low-molecular-weight proteins are not the result of a post-translational cleavage of the largest. All were distinctly different from the whey protein alpha-lactalbumin.


1964 ◽  
Vol 17 (4) ◽  
pp. 283-285
Author(s):  
Takao Shinagawa ◽  
Toshio Habu ◽  
Akemi Murakami

2019 ◽  
Vol 18 (1) ◽  
pp. 85-91
Author(s):  
AI Kriukova ◽  
IM Vladymyrova ◽  
OL Levashova ◽  
TS Tishakova

The amino acid composition of the roots of Harpagophytum procumbens was investigated by the method of high performance liquid chromatography (HPLC) with preliminary derivatization. Sixteen free and thirteen bound amino acids were quantitatively determined. The content of protein-bound amino acids was calculated. Dhaka Univ. J. Pharm. Sci. 18(1): 85-91, 2019 (June)


2020 ◽  
Vol 58 (8) ◽  
pp. 687-694
Author(s):  
Kumarswamy Ummiti ◽  
J V Shanmukha Kumar

Abstract Ganirelix is a synthetic decapeptide linked with nine different amino acids. To understand the peptide amino acid sequence or primary structure, the first step is to determine the amino acid composition of the peptide which can be a determining factor for the peptide immunogenicity. Edman degradation is not a suitable analytical technique to identify amino acid sequence present in Ganirelix due to the absence of uncharged N-terminal amino group. To address this challenge, a pre-column derivatization method was developed with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent. In the present work, the Ganirelix active pharmaceutical ingredient present in the injectable formulation was isolated by fraction collection and further purified by flash chromatography. The amino acid composition of Ganirelix is assayed by carrying out acid hydrolysis with 6 mol L−1 hydrochloric acid solution containing 1% phenol at 100°C for 24 h and derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate reagent solution, followed by determination of individual amino acids by reverse-phase chromatography using a C18 column. High resolution was achieved for the nine amino acid mixture. The amino acid composition results of temperature-stressed Ganirelix generic product and reference listed drug are in good agreement with the theoretical molar ratio of label information.


Author(s):  
Г.А. ОСИПОВА ◽  
Н.А. БЕРЕЗИНА ◽  
Т.В. СЕРЕГИНА ◽  
А.Е. ЖУГИНА

Цель настоящего исследования – повышение биологической ценности макаронных изделий путем использования белоксодержащих обогащающих добавок растительного и животного происхождения. Обогащающие добавки: мясные продукты – мясо кур (грудная часть тушки) и телятину I категории охлажденную; муку бобовых культур – соевую дезодорированную полуобезжиренную, гороховую и чечевичную; изоляты соевого, горохового и кукурузного белков – добавляли в макаронное тесто, приготовленное по традиционной технологии из муки пшеничной хлебопекарной высшего сорта (ГОСТ Р 52189–2003). Установлено, что для обогащения макаронных изделий рациональны дозировки добавок: мясных 15% от массы муки; гороховой и чечевичной муки и растительных изолятов 10% от массы смеси; соевой муки 7,5% от массы смеси. Выявлено положительное влияние вносимых в макаронное тесто обогащающих добавок на увеличение содержания белка в составе изделий на 1,59–8,19%, повышение сбалансированности аминокислотного состава белков, их биологической ценности на 6–16%, значений коэффициентов утилитарности аминокислотного состава на 0,2–0,26 дол. ед., перевариваемости белков под действием протеолитического фермента пепсина на 11–24%, степени удовлетворения суточной потребности в белке на 1,5–13,4% по сравнению с контрольным образцом без добавок. На макаронные изделия с обогащающими белоксодержащими добавками разработана и утверждена техническая документация – технические условия, технологические инструкции и рецептуры. The purpose of this study is to increase the biological value of pasta by using protein-containing enriching additives of plant and animal origin. Enriching additives: meat products-chicken meat (breast part of the carcass) and veal category I chilled; bean flour – soy deodorized semi-skimmed, pea and lentil; isolates of soy, pea and corn proteins – added to pasta dough prepared according to traditional technology from wheat flour bakery of the highest grade (GOST R 52189–2003). It has been established that the enrichment of pasta products of the rational will of a dosage of the additives: meat 15% by weight of flour; pea and lentil flour and vegetable isolates 10% by weight of the mixture; soya flour is 7,5% by weight of the mixture. The positive effect of the enriching additives introduced into the macaroni dough on the increase in the protein content in the products by 1,59–8,19%, the increase in the balance of the amino acid composition of proteins, their biological value by 6–16%, the values of the utilitarian coefficients of the amino acid composition by 0,2–0,26 units, the digestibility of proteins under the action of the proteolytic enzyme pepsin by 11–24%, the degree of satisfaction of the daily protein demand by 1,5–13,4% compared to the control sample without additives was revealed. Technical documentation – technical specifications, technological instructions and recipes has been developed and approved for pasta with protein-containing additives.


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