Studies of the reaction between proteins and reducing sugars in the ‘dry’ state II. Further observations on the formation of the casein-glucose complex

Lea, C. H.; Hannan, R.S.

doi:10.1016/0006-3002(50)90058-8

Cited by 96 publications

(24 citation statements)

References 14 publications

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“…25 The decrease in lysine during conjugation of caseinate and fructose was considerably faster at a 1:5 (ratio of lysine residues to sugar carbonyl groups) than a 1:2.5, particularly at 60 • C and above (Figs 3 and 4). This was in contrast to the studies of Lea and Hannan, 26 which showed an optimal reaction between caseinate and glucose at 1:3 amino:carbonyl group equivalents. On the other hand, at the higher temperature of 60 • C used in the present study versus the 37 • C used by Lea and Hannan, 26 it can be expected that a greater concentration of Maillard reaction products will be formed.…”

Section: Effect Of Fructose Concentration Inulin and Temperaturecontrasting

confidence: 53%

“…This was in contrast to the studies of Lea and Hannan, 26 which showed an optimal reaction between caseinate and glucose at 1:3 amino:carbonyl group equivalents. On the other hand, at the higher temperature of 60 • C used in the present study versus the 37 • C used by Lea and Hannan, 26 it can be expected that a greater concentration of Maillard reaction products will be formed. Many of these products, for example the α-dicarbonyl compounds, are known to have greater reactivity than the original sugar molecules.…”

Section: Effect Of Fructose Concentration Inulin and Temperaturecontrasting

confidence: 53%

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Glycation of caseinate by fructose and fructo‐oligosaccharides during controlled heat treatment in the ‘dry’ state

Oliver¹,

Melton²,

Stanley³

2005

J Sci Food Agric

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This paper investigates the controlled heating of caseinate with reducing sugars to produce glycoproteins with improved functionality for use in food. Caseinate was combined with inulin, fructose and a mixture of both inulin and fructose and the lyophilisates heated at a controlled water activity for up to 48 h. Caseinate-glucose and caseinate-lactose glycoconjugates were prepared for comparison. Conjugation between caseinate and fructose occurred readily at 60 • C and 67% relative humidity, modifying up to 75% of the lysine groups of caseinate within 48 h. Moreover, when reconstituted, the caseinate-fructose glycoconjugates showed a dramatic increase in viscosity relative to caseinate 'dry'-heated alone. At 80% relative humidity the reaction proceeded so rapidly that gels containing darkly coloured particulate matter were formed. Incorporation of inulin prevented formation of caseinate-fructose gels, and minimised browning development while still producing moderately viscous solutions. Based on 13 C-NMR, SDS-PAGE and electron microscopy techniques, mechanisms by which inulin modified the reaction have been proposed.

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Section: Effect Of Fructose Concentration Inulin and Temperaturecontrasting

confidence: 53%

Section: Effect Of Fructose Concentration Inulin and Temperaturecontrasting

confidence: 53%

Glycation of caseinate by fructose and fructo‐oligosaccharides during controlled heat treatment in the ‘dry’ state

Oliver¹,

Melton²,

Stanley³

2005

J Sci Food Agric

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“…It decreases nutritional value due to blocking of lysine and other essential amino acids (Malec et al, 2002;Pizzoferrato et al, 1998). It may cause off-flavor development (Morr and Ha, 1991;Walker, 1972), poor protein solubility (Kato et al, 1986;Hannan, 1949 and1950), and decreased digestibility (Culver and Swaisgood, 1989), produce adverse browning (Guerra-Hernandez et al, 2002;Saio et al, 1980), and shorten product shelf-life (Albalá-Hurtado et al, 1999;Guyomarc'h et al, 2000;Stapelfeldt et al, 1997;Van Mill and Jans, 1991).…”

Section: Protein Glycationmentioning

confidence: 95%

Creating Proteins with Novel Functionality via the Maillard Reaction: A Review

Oliver

Melton

Stanley

2006

Critical Reviews in Food Science and Nutrition

432

299

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Proteins are widely utilized to add functional properties, such as gelling and emulsification to foods. These attributes depend on a number of factors such as molecular structure of the protein, the pH, and the composition of its chemical environment. There is substantial evidence to suggest that the functional properties of food proteins can be further improved by derivatization. Covalent bonding of proteins to polysaccharides and smaller reducing sugars via the Maillard reaction has been shown to alter the functionality of proteins without requiring the addition of chemical reagents. Establishment of a technologically feasible method for preparing the conjugates and optimization of the processing conditions, however, is needed to promote their development as functional food ingredients. This paper provides a state-of-the-art contribution to the impact of the Maillard reaction on protein functionality. It presents a deeper understanding of the influence of processing conditions and reactant formulation on improving desirable properties of proteins. In particular attention is given to how potential improvements could be achieved in the emulsifying, textural, and solubility properties of proteins to add value to commodity food ingredients. Elements that are considered to be critical to the design of functional Maillard conjugates are highlighted and suggestions proposed to facilitate progress in this area.

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“…This was a commercial sample further purified by the method of Lea & Hannan (1950). A 3-28 % solution was used for inoculation.…”

Section: Bacterial Suspensionsmentioning

confidence: 99%

The conglutination phenomenon IX. The production of immuno-conglutinin in rabbits

Coombs

1953

Epidemiol. Infect.

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1. An investigation has been carried out into the conditions necessary for the production of immuno-conglutinin in rabbits.2. The inoculation of complement adsorbed on sensitized cells stimulates the production of immuno-conglutinin. We have called this procedure hetero-stimulation.3. Immuno-conglutinin also results from the inoculation of untreated but killed bacteria. This procedure for its production we call auto-stimulation. Gram-negative bacteria appear to be more effective stimulants than Gram-positive bacteria. Soluble antigens did not appear to be as effective as bacterial suspensions.4. The necessity for clarifying the part played by immuno-conglutinin in in vivo immune processes has been stressed.The authors would like to thank the following for gifts of experimental materials: Mr H. I. Field, strains of S. pullorum; Dr J. Boissard, strain of C. hofmanni; Dr C. H. Lea and Dr R. S. Hannan, purified casein; Miss Dunkerley, Bence Jones protein. Cx polysaccharide for testing acute phase protein in rabbit serum was made available by the kindness of Dr McCarty of the Hospital of the Rockefeller Institute for Medical Research, New York; and much of the work on this aspect was done in consultation with Dr H. C. Anderson, to whom we are most grateful.

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Studies of the reaction between proteins and reducing sugars in the ‘dry’ state II. Further observations on the formation of the casein-glucose complex

Cited by 96 publications

References 14 publications

Glycation of caseinate by fructose and fructo‐oligosaccharides during controlled heat treatment in the ‘dry’ state

Glycation of caseinate by fructose and fructo‐oligosaccharides during controlled heat treatment in the ‘dry’ state

Creating Proteins with Novel Functionality via the Maillard Reaction: A Review

The conglutination phenomenon IX. The production of immuno-conglutinin in rabbits

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