Maillard reaction in vivo and its relevance to diseases: editorial and dedication

The antioxidant and anti-browning activity of heated plant extracts have been attributed to the formation of Maillard reaction products (MRPs) via the Maillard reaction (MR). The inhibitory effect of heated Moringa oleifera (MO) seed extract on banana polyphenol oxidase (PPO) was investigated. The Plain MO seed extracts and those with added glucose and glycine (1.5 mM each) were heated at 100°C for 15, 30, 60 and 120 min. The pH and brown colour development decreased and increased significantly (P <0.05) with increased reaction time, respectively, with heated moringa glucose-glycine HMGGL for 120 min exhibiting the highest pH reduction (2.58) and darkest extracts at an L* value of 8.11. This phenomenon is associated with progression of the MR. With reference to enzymatic browning, heated MO seed extracts exhibited stronger inhibitory effect against banana PPO activity in vivo and in vitro than the unheated counterpart. Evident to this are the higher inhibition percentages and lower ΔE values. Among model systems, the highest in vitro browning inhibition was exhibited mostly by longer heating times of 60 and 120 min. Model system HMGGL 120 min proved to be superior at 96% inhibition, which was comparable to known synthetic commercial antioxidants such as ascorbic acid (AA) at 99%, as well as ethylenediaminetetraacetic acid (EDTA) and citric acid (CA), both at 100% inhibition. In vivo enzymatic browning inhibition followed a similar trend, where the brown pigment (melanin) intensified as shown by an increase in ΔE as the storage time increased from 0.5 to 24 h. The model system UMGGL exhibited highest inhibition of brown melanin (p <0.05). Although it was the best amongst other model systems, it was surpassed by synthetic antioxidants AA, EDTA and CA, which were ranked amongst the top three in inhibiting brown pigment formation in vivo. To further illustrate the effect of MR augmented MO seed extracts on enzyme activity inhibition, UMGGL 60 and 120 at 5 and 24 h storage surpassed the inhibitory effect of AA. At the said storage times, AA lost its inhibitory potential against pigment formation. This was due to oxidation of AA to form dehydroascorbic acid, which lacks inhibitory potential. This study proved that heating MO plant extracts increases their enzymatic browning inhibition potential, furthermore, the inhibitory capacity was heightened when reacted via the MR.

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Determination of Dicarbonyl Compounds as Aminotriazines during the Maillard Reaction and in Vivo Detection in Aminoguanidine-Treated Rats

The Maillard Reaction in Foods and Medicine ◽

10.1533/9781845698447.8.400a ◽

2005 ◽

pp. 400 ◽

Cited By ~ 1

Author(s):

Atsushi Araki ◽

Marcus A Glomb ◽

Motoko Takahashi ◽

Vincent M Monnier

Keyword(s):

Maillard Reaction ◽

Dicarbonyl Compounds ◽

In Vivo Detection

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Evidence against the formation of 2-amino-6-(2-formyl-5-hydroxymethyl-pyrrol-l-yl)-hexanoic acid ('pyrraline') as an early-stage product or advanced glycation end product in non-enzymic protein glycation

Clinical Science ◽

10.1042/cs0840087 ◽

1993 ◽

Vol 84 (1) ◽

pp. 87-93 ◽

Cited By ~ 16

Author(s):

Patricia R. Smith ◽

Hanif H. Somani ◽

Paul J. Thornalley ◽

Jonathan Benn ◽

Peter H. Sonksen

Keyword(s):

Maillard Reaction ◽

Early Stage ◽

Hexanoic Acid ◽

Protein Glycation ◽

Advanced Glycation ◽

Keyhole Limpet Haemocyanin ◽

Advanced Glycation End Product ◽

Physiological Conditions

1. It has been suggested that 2-amino-6-(2-formyl-5-hydroxymethyl-pyrrol-l-yl)-hexanoic acid ('pyrraline') is formed as an advanced glycation end product in the Maillard reaction under physiological conditions. Antibodies were raised to caproyl-pyrraline linked to keyhole-limpet haemocyanin and were used to develop an e.l.i.s.a. and Western blotting system for the specific detection of pyrraline in samples in vivo and in vitro. 2. Human serum albumin was isolated from the serum samples of diabetic and non-diabetic subjects. Pyrraline was not detected (<1.2 pmol) in any of the samples, indicating that it was not a major advanced glycation end product in vivo. 3. BSA was incubated separately with D-glucose and a model fructosamine, N-(l-deoxy-D-fructos-l-yl)-hippuryl-lysine, under physiological conditions for 30 days. Aliquots removed from the incubations at 5 day intervals contained no detectable pyrraline, indicating that pyrraline was not an early-stage product of the Maillard reaction in vitro. 4. The model fructosamine, N>-(1-deoxy-D-fructos-l-yl)-hippuryl-lysine, was incubated at pH 7.4 and 37°C for 25 days during which it degraded to hippuryl-lysine and N>-carboxymethyl-hippuryl-lysine. Aliquots were removed at 5 day intervals and assayed for pyrraline. None was detected (<23 pmol/ml) in the course of the degradation of the fructosamine (400 nmol/ml degraded), indicating that pyrraline was not a major product of the degradation of fructosamine under physiological conditions in vitro. 5. We conclude that pyrraline is not a major intermediate or advanced glycation end product in the Maillard reaction under physiological conditions in vitro and in vivo. A previous report of immunoassay of pyrraline may have given positive results because of non-specific antibodies raised to impure hapten.

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