The reaction between proteins and reducing sugars in the ‘dry’ state. Relative reactivity of the α- and ∈-amino groups of insulin

Schwartz, H. M.; Lea, C. H.

doi:10.1042/bj0500713

Cited by 41 publications

(13 citation statements)

References 9 publications

(5 reference statements)

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“…The greater effects of autoclaving on AID and SID of all AA than of oven drying are, therefore, probably due to the pressure and moisture that are associated with autoclaving. Amino acids are less stable at greater pressure (Qian et al, 1993), and the rate of reaction between the amino group of AA and glucose increases if the humidity is increased (Schwartz and Lea, 1952). The development of Maillard reactions depends on water activity, temperature, pH, time of heating, and the type and availability of the reactants (Rufián-Henares et al, 2009;Jaeger et al, 2010).…”

Section: Discussionmentioning

confidence: 98%

Amino acid digestibility in heated soybean meal fed to growing pigs1

González-Vega

Kim

Htoo

et al. 2011

Journal of Animal Science

151

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Heat treatment of soybean meal (SBM) is necessary to reduce the concentration of trypsin inhibitors, but excessive heat treatment may reduce AA concentration and digestibility because AA can be destroyed by the Maillard reaction. The objective of this experiment was to determine the effects of heat treatment of SBM on apparent ileal digestibility and standardized ileal digestibility (SID) of AA by growing pigs. A source of conventional dehulled SBM (48.5% CP) was divided into 4 batches. One batch was not additionally heated, 1 batch was autoclaved at 125°C for 15 min, 1 batch was autoclaved at 125°C for 30 min, and 1 batch was oven-dried at 125°C for 30 min. Four SBM-cornstarch diets were formulated, and each of the 4 batches of SBM was used as the sole source of dietary AA in 1 diet. A N-free diet was used to estimate basal endogenous losses of AA. Ten growing barrows with an initial BW of 25.3 ± 2.0 kg were individually fitted with a T-cannula in the distal ileum. Pigs were allotted to treatments in a replicated 5 × 5 balanced Latin square design with 5 diets and 5 periods. Each period lasted 7 d, and ileal digesta were collected on d 6 and 7 of each period. Results of the experiment indicated that the apparent ileal digestibility and SID of CP and all AA decreased linearly (P < 0.01) as the time of autoclaving increased from 0 to 30 min. The concentration of furosine and the color of samples of SBM indicated that autoclaving resulted in a Maillard reaction in the SBM. However, oven drying at 125°C for 30 min did not change (P > 0.10) the SID of CP and AA in the SBM or the furosine concentration, and the color in the oven-dried sample indicated that this sample was not heat damaged. In conclusion, the digestibility of all AA in autoclaved SBM is linearly reduced as the autoclaving time increases from 0 to 30 min. The reason for these changes is most likely that autoclaving at 125°C results in Maillard reactions in SBM.

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Section: Discussionmentioning

confidence: 98%

Amino acid digestibility in heated soybean meal fed to growing pigs1

González-Vega

Kim

Htoo

et al. 2011

Journal of Animal Science

151

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“…At low moisture levels, the Maillard reaction is less rapid because the diffusion and mobility of reactants are restricted. 2,34,52 As water content increases, molecular mobility increases, leading to enhanced reactant mobility which should facilitate the reaction. 37 At higher water contents, the reaction rates decrease due to dilution of the reactants by water.…”

Section: Factors Influencing Protein and Peptide Chemical Instabilitymentioning

confidence: 99%

Solid‐state chemical stability of proteins and peptides

Lai¹,

Topp

1999

Journal of Pharmaceutical Sciences

251

145

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Peptide and protein drugs are often formulated in the solid-state to provide stabilization during storage. However, reactions can occur in the solid-state, leading to degradation and inactivation of these agents. This review summarizes the major chemical reactions affecting proteins and peptides in the solid-state: deamidation, peptide bond cleavage, oxidation, the Maillard reaction, beta-elimination, and dimerization/aggregation. Physical and chemical factors influencing these reactions are also discussed. These include temperature, moisture content, excipients, and the physical state of the formulation (amorphous vs crystalline). The review is intended to serve as an aid for those involved in formulation, and to stimulate further research on the determinants of peptide and protein reactivity in the solid-state.

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“…It is also of interest that the data follow the rate curve for an amine of pK 6.9, since this agrees within experimental error with the pK of N-terminal phenylalanine, which Schwartz and Lea (1952) found to be the most reactive site in insulin. Although the formation of a Schiff base on the protein may be the rate-limiting reaction in this system, it is considered more likely that the structure of the isolated reaction product would be the cyclic glycosylamine or even the Amadori product (Reynolds, 1963).…”

Section: And Discussionmentioning

confidence: 83%

“…The reactions between aldoses and proteins in the "dry" state were intensively investigated over a decade ago by Lea and co-workers Hannan, 1949, 1950;Lea and Rhodes, 1952;and Lea et al, 1951) with respect to the effect of moisture content and pH on the rate of loss of free aminogroups on the protein, and by Haugaard and Tumerman (1956) on the rate of reaction of amino groups in proteins in solution. The reaction between insulin and glucose has been studied (Schwartz and Lea, 1952) This paper introduces a new approach to the general problem of the reaction of aldoses and proteins in which it is feasible to study the reaction at very low aldose concentrations with respect to the reactive groups on the protein, a situation which is of importance with respect to many dehydrated protein foods. As will be seen, it was also possible to isolate from the complex browning reaction pathway the very earliest stages involved in the binding of glucose to insulin.…”

Section: Introductionmentioning

confidence: 99%

Protein Carbonyl Browning Systems: A Study of the Reaction Between Glucose and Insulin

Tannenbaum

1966

Journal of Food Science

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SUMMARY The interaction between glucose and insulin in the dry state was studied at a relatively low glucose concentration with carbon‐14‐labeled glucose. The conditions of the investigation were that the equilibrium relative humidity was 0.74, pH range 4–7, and temperature range 35–55°C. Under these conditions, the rate of the reaction decreased with increasing pH and had an activation energy of approximately 2.7 Kcal/mole. Reasons are given for believing that the reaction may be the formation of a Schiff base.

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The reaction between proteins and reducing sugars in the ‘dry’ state. Relative reactivity of the α- and ∈-amino groups of insulin

Cited by 41 publications

References 9 publications

Amino acid digestibility in heated soybean meal fed to growing pigs1

Amino acid digestibility in heated soybean meal fed to growing pigs1

Solid‐state chemical stability of proteins and peptides

Protein Carbonyl Browning Systems: A Study of the Reaction Between Glucose and Insulin

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