Changes to amino acid composition of bloodmeal after chemical oxidation

RSC Advances ◽  
2015 ◽  
Vol 5 (81) ◽  
pp. 66451-66463 ◽  
Author(s):  
T. M. Hicks ◽  
C. J. R. Verbeek ◽  
M. C. Lay ◽  
M. Manley-Harris
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Weight Distribution ◽  
Peracetic Acid ◽  
Protein Solubility ◽  
Chemical Oxidation ◽  
Chemical Characteristics ◽  
Physical And Chemical

The effect of oxidative decolouring with peracetic acid on the physical and chemical characteristics of bloodmeal proteins was investigated by assessing protein solubility, molecular weight distribution and final amino acid composition.

scholarly journals Functional Properties of Extracted Protein from Edible Insect Larvae and Their Interaction with Transglutaminase

Foods ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 591 ◽  
Author(s):  
Tae-Kyung Kim ◽  
Hae In Yong ◽  
Hae Won Jang ◽  
Young-Boong Kim ◽  
Yun-Sang Choi
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Molecular Weight Distribution ◽  
Acid Composition ◽  
Incubation Time ◽  
Weight Distribution ◽  
Protein Solutions ◽  
Cross Linking ◽  
Edible Insect

Global concern about food supply shortage has increased interest on novel food sources. Among them, edible insects have been studied as a potential major food source. This study aimed to improve the functional properties of protein solutions extracted from Protaetia brevitarsis (PB) by use of transglutaminase (TG) as a cross-linking agent. After various incubation times (10, 20, 30, 60, and 90 min) with TG, the protein solutions were assessed with regard to their amino acid composition, protein nutritional quality, pH, color (yellowness), molecular weight distribution, thermal stability, foam ability (capacity and stability), and emulsion ability (capacity and stability). Incubation with TG changed the amino acid composition of the proteins and shifted the molecular weight distribution towards higher values, while improving the rest of the aforementioned properties. Since the incubation time for 90 min decreased the protein functionality, the optimum incubation time for cross-linking PB-derived protein with TG is 60 min. The application of TG to edible insect proteins ultimately increases its functionality and allows for the development of novel insect processing technology.

Amino acid composition and molecular weight of Botrytis cinerea laccase

1977 ◽  
Vol 16 (7) ◽  
pp. 1051-1052 ◽  
Author(s):  
Alfred M. Mayer ◽  
Irith Marbach ◽  
Assa Marbach ◽  
Ada Sharon
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Botrytis Cinerea ◽  
Acid Composition

scholarly journals Separation and partial characterization of guinea-pig caseins

1978 ◽  
Vol 173 (2) ◽  
pp. 633-641 ◽  
Author(s):  
R K Craig ◽  
D McIlreavy ◽  
R L Hall
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Guinea Pig ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Exchange Chromatography

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.

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