Mechanisms of heat damage in proteins. 2. Chemical changes in pure proteins.

@article{Bjarnason1970MechanismsOH,
  title={Mechanisms of heat damage in proteins. 2. Chemical changes in pure proteins.},
  author={J{\'o}n Bragi Bjarnason and Kenneth J. Carpenter},
  journal={The British journal of nutrition},
  year={1970},
  volume={24 1},
  pages={
          313-29
        }
}
1. Bovine plasma albumin (BPA) containing approximately 14% moisture, when heated for 27 h at 115° suffered an appreciable loss of cystine and a small loss of lysine; at 145° all the amino acids except glutamic acid and those with paraffin side-chains, showed considerable losses. Isoleucine also showed some loss through racemization to alloisoleucine. 2. BPA heated at 115° evolved H 2 S; at 145° other sulphur compounds were released as well, all coming from the breakdown of cystine. Possible… Expand
Mechanisms of heat damage in proteins. 7. The significance lysine-containing isopeptides and of lanthionine in heated proteins.
TLDR
Studies have been made with solvent-extracted chicken muscle, bovine plasma albumin (BPA) and other proteins, all severely heated in the absence of carbohydrates so as to cause a large decrease in their fluorodinitrobenzene (FDNB)-reactive lysine contents, and there was some difficulty in quantifying the amounts of isopeptides formed on heat treatment. Expand
Metabolism of heat-damaged proteins in the rat. influence of heat damage on the excretion of amino acids and peptides in the urine.
TLDR
In urine of rats given protein isolated from heated skim-milk powder, the peptide hydro-lysate was rich in lysine and in furosine, which together comprised 41 mol % of the total amino acid composition. Expand
Mechanisms of heat damage in proteins. 5. The nutritional values of heat-damaged and propionylated proteins as sources of lysine, methionine and tryptophan.
TLDR
The effects of this treatment on amino acid composition and availability are compared with the effects of severe heat treatment (autoclaving) of a protein and the merits of microbiological estimates of amino acid availability are assessed. Expand
The use of three dye-binding procedures for the assessment of heat damage to food proteins.
TLDR
Animal feeding-stuffs, whether unheated, industrially processed or diliberately heated, appeared to react with Acid Orange 12 in the same way as the model systems (selected to represent three types of heat damage: 'advanced' and 'early' Maillard and protein-protein damage). Expand
Mechanisms of heat damage in proteins. 6. The digestibility of individual amino acids in heated and propionylated proteins.
TLDR
It appears that reduced digestibility is an adequate explanation for the reduction found in nutritional value of the autoclaved protein, and the type of dietary protein used did influence the amino acid composition of the ileal contents. Expand
The participation of methionine and cysteine in the formation of bonds resistant to the action of proteolytic enzymes in heated casein.
TLDR
It was concluded that the oxidation of casein causes the formation of complexes in the polypeptide chain, resistant to enzymic hydrolysis, but to a much lesser extent than does heating. Expand
Behavior of O-glycosyl and O-phosphoryl proteins in alkaline solution.
TLDR
For these studies, two unique proteins were used: phosvitin, a well-characterized protein with 120 0-phosphoryl groups and no cystine or 0-glycosyl groups; and a glycopeptide related to the antifreeze protein from Antarctic fish, aWell-Characterized protein consisting of (Ala-Ala -Thr)n in which all of the threonyl residues are glycosylated. Expand
Specific limited hydrolysis and phosphorylation of food proteins for improvement of functional and nutritional properties
Limited specific hydrolysis of casein byStaphylococcus aureus V8 protease was used to produce 2% and 6.7% hydrolysates (2 and 6.7% of the peptide bonds hydrolyzed), each containing five polypeptidesExpand
Nutritional significance of cross-link formation during food processing.
When proteins are severely heated, in the presence or absence of sugars, the fall in nutritional value appears to be largely, although not completely, explained by reduced protein digestibility. AllExpand
The role of glutamic acid/glutamine and lysine during nondashenzymic browning in heated gluten
Abstract During dry heat processing of a crude gluten preparation (c. 75% protein) at 160°C for 30 min, about 25% of the available lysine and 10% of the glutamine residues are lost with the evolutionExpand
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TLDR
Giving a pure protein in which the nutritional availability of the lysine had been reduced heat treatment resulted in greatly increased faecal lysins but little urinary lysines, suggesting that the compounds themselves were appearing in the urine. Expand
Damage to proteins, enzymes, and amino acids by peroxidizing lipids.
Abstract Transient free-radicals are produced in peroxidizing lipid-protein reaction systems. The pattern of damage to proteins, induced by these radicals, is similar to that observed in the case ofExpand
The N-terminal sequence of serum albumins; observations on the thiohydantoin method.
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TLDR
The FDNB method has been successfully used and it is theoretically possible to proceed down the chain with small quantities of material, provided that a highly selective method for the cleavage and cyclization of the phenylthiocarbamyl (PTC) derivative is available and that good yields are obtained at each stage. Expand
Availability of sulphur amino acids in protein foods. 4. Effect of heat treatment upon the total amino acid content of cod muscle.
TLDR
The finding has been that the composition of two preparations of cod muscle, heated in different ways so as to produce large reductions in protein quality, differed from the compositions of the control material only by relatively small changes in a few amino acids. Expand
On the sequence of residues 11 to 18 in bovine pancreatic ribonuclease.
TLDR
A thorough reinvestigation of the sequence in this part of the molecule was undertaken and it was established that the correct sequence from positions 11 to 18 is GluNHrHis-MetAsp-Ser- Ser-Thr-Ser. Expand
Analysis of enzymically digested food proteins by sephadex-gel filtration.
TLDR
The present paper describes the application of Sephadex-gel filtration, combined with microbiological assays, in a study of the effects of heating on the biological availability of some amino acids in fish protein. Expand
The differential determination of lysine in heated milk. I. In vitro methods.
TLDR
A nomograph is presented which accounts for the different conditions of lysine in heated milk and allows the interconversion of the x, y, z and v-values. Expand
On the structure of alpha-lactalbumin. I. Degradation studies with carboxypeptidase A and carboxypeptidase B.
TLDR
Tryptic digestion of α-lactalbumin resulted, in addition to the peptide fragments, in ihe liberation of free lysine and leucine in stoichionietric amounts, and Cleavage of the disulfide bridges of α -lact Albumin did not change the molecular weight of the protein. Expand
Configuration of certain protein molecules. An inquiry concerning the present status of our knowledge
It is now becoming possible to correlate studies on the general size and shape of protein molecules in solution with knowledge of the possible configurations of polypeptide chains and, in someExpand
Nδ-(2d-amino-2-carboxyethyl)-ornithine, a New Amino-acid from Alkali-treated Proteins
A NEW amino-acid, N ε-(2-amino-2-carboxyethyl)-lysine, in acid hydrolysates of alkali-treated proteins has been reported1,2. The trivial name lysinoalanine was chosen for this compound, which isExpand
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