Isolation and characterization of pigments from protein-carbonyl browning systems.  Models for two insulin-glucose pigments

Clark, Allen V.; Tannenbaum, Steven R.

doi:10.1021/jf60196a002

Cited by 35 publications

(23 citation statements)

References 15 publications

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“…Hofmann (1998) reported that the reaction between casein and glucose led to a drastic increase in the MWs by carbohydrate-induced oligomerisation of the protein backbone. Furthermore, these results confirm the earlier findings of Clark and Tannenbaum (1974) that the reaction between proteins and carbohydrates leads to polymerisation of the reaction mixture. The results showed that the shapes of the chromatogram of MRPs derived from the Glu-Di and Glu-Tri model systems were different from those of MRPs derived from the Glu-G model system as the heating time increased.…”

Section: Evolution Of Mw In Mrpssupporting

confidence: 91%

Study of Maillard reaction products derived from aqueous model systems with different peptide chain lengths

Kim

Lee

2009

Food Chemistry

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Section: Evolution Of Mw In Mrpssupporting

confidence: 91%

Study of Maillard reaction products derived from aqueous model systems with different peptide chain lengths

Kim

Lee

2009

Food Chemistry

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“…Hofmann (29) reported that the reaction between casein and glucose led to a drastic increase in molecular weights by carbohydrate-induced oligomerization of the protein backbone. Furthermore, these results confirm the earlier findings of Clark and Tannenbaum (30) that the reaction between proteins and carbohydrates leads to polymerization of the reaction mixture. The results showed that the melanoidins formed from BG after different thermal processing steps had different size exclusion chromatography elution patterns.…”

Section: Resultssupporting

confidence: 91%

Evaluation of Melanoidins Formed from Black Garlic after Different Thermal Processing Steps

Kang

2016

JFN

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The objective of this study was to evaluate the characteristics of melanoidins formed from black garlic (BG) after different thermal processing steps. The melanoidins formed from BG during thermal processing were produced in large amounts, and the initial (280 nm), intermediate (360 nm), and final stage product (420 nm) had similar tendencies. Compounds like degraded proteins, peptides, and phenolic acids were present in the melanoidins during thermal processing. All the melanoidin samples showed different absorptions in the UV-visible spectra, although these had similar shapes. Moreover, the carbon, hydrogen, and oxygen content of melanoidins formed from BG during thermal processing decreased initially, and then increased. However, the nitrogen content increased during thermal processing. As thermal processing progressed, the molecular weight of all the melanoidin samples showed increasing intensities, whereas the major peaks of each melanoidin sample had different retention times. Furthermore, the melanoidins formed from BG after different thermal processing steps contained -OH, -CH, amide I, and III groups. The crystallinity of the melanoidins was majorly formed at 31.58° and 43.62° (2θ).

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“…Other tissues that contain long-lived proteins, such as lens and nerve, might be affected by nonenzymatic browning as well. Isolation and structural analyses of protein pigments are required to further substantiate the browning concept and indicate more specifically how these modified proteins might play a role in the pathogenesis of the complications of diabetes and aging (31)(32)(33). In addition, further understanding of nonenzymatic browning in vivo is needed so that strategies for interfering with the process on long-lived proteins can be devised.…”

Section: Discussionmentioning

confidence: 99%

Accelerated age-related browning of human collagen in diabetes mellitus.

Monnier

Kohn

Cerami

1984

Proc. Natl. Acad. Sci. U.S.A.

624

355

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The nonenzymatic glycosylation reaction that is accelerated in diabetes is the first step of the Maillard or nonenzymatic browning reaction that occurs in stored food. The glucose-protein adduct rearranges and dehydrates to form brown and fluorescent pigments, which can act as crosslinks, resulting in decreased protein solubility and altered mechanical properties. Evidence suggesting that this process occurs in vivo has been found in lens crystallins. The observation that nonenzymatic glycosylation and insolubility increases in collagen with age and diabetes led us to investigate the possible browning of human collagen. Several complications of diabetes mellitus occur in collagenrich tissues and resemble processes and diseases characteristic of aging. These include earlier onset and greater severity of atherosclerosis (1), stiffening of lungs (2) and large arteries (3, 4), thickening of capillary and glomerular basement membranes (5, 6), periarticular rigidity (7), and osteoarthritis (8). With age, collagen becomes less soluble (9, 10), more crosslinked (11), and more glycosylated (10,12), and it accumulates yellow and fluorescent pigments (13,14). In diabetes, several of these changes occur at an earlier age, suggesting an apparent acceleration of the aging process. Compared with age-matched nondiabetics, collagen from diabetics is less soluble (10), is more resistant to digestion by collagenase (15) and cyanogen bromide (16), has more pepsin-releasable high molecular weight peptides (10), and is more nonenzymatically glycosylated (10,15,17). Glycosylation and subsequent crosslinking occur in food proteins that are stored or heated in the presence of reducing sugars and are due to the Maillard or nonenzymatic browning reaction. Glucose, for example, first reacts nonenzymatically with free amino groups on proteins to form a stable amino 1-deoxyketosyl adduct, also called the Amadori product. Nonenzymatic glycosylation has been shown to occur with hemoglobin to form hemoglobin Al, and with a variety of other body proteins-e.g., lens crystallins, collagen, and nerve proteins (18 proteins (20). The recent demonstration that insolubility and resistance to enzymatic digestion of human collagen increase with age and diabetes in parallel with nonenzymatic glycosylation (10) led to the present investigation of the browning process in the same subject population. Insoluble dura mater collagen from nondiabetics and subjects with type I and type II diabetes was examined for the presence of yellow and fluorescent pigments similar to those that form in the nonenzymatic browning reaction with glucose. MATERIAL AND METHODSThe samples of dura mater used in this study were obtained at autopsy from the same subjects in whom age-and diabetes-related changes in skin collagen solubility and glycosylation were reported by Schnider and Kohn (10). These include 17 samples of dura mater from subjects without clinical or pathological evidence of connective tissue disease or diabetes mellitus and similar samples from 3 subjects w...

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Isolation and characterization of pigments from protein-carbonyl browning systems. Models for two insulin-glucose pigments

Cited by 35 publications

References 15 publications

Study of Maillard reaction products derived from aqueous model systems with different peptide chain lengths

Study of Maillard reaction products derived from aqueous model systems with different peptide chain lengths

Evaluation of Melanoidins Formed from Black Garlic after Different Thermal Processing Steps

Accelerated age-related browning of human collagen in diabetes mellitus.

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