Loss Of Fructose Research Articles

Characteristics and antioxidant activity of Maillard reaction products from fructose-glycine oligomer

The pH of Maillard reaction products (MRPs) derived from the Gly model system (Gly) decreased markedly as heating time increased. However the Digly model system (Digly) exhibited the highest increase in absorbance at 294 and 420 nm. Moreover, the loss of fructose and degree of sugar enolization in MRPs derived from the Trigly model system (Trigly) was the highest, whereas the glycine oligomer content in the Digly noticeably decreased as heating time increased. Furthermore, the gel permeation chromatograms (GPC) patterns of all MRP samples exhibited rising intensities as a function of the heating time, whereas the major peaks of each MRP sample were eluted at different retention times as glycine oligomer. Antioxidant activity of each MRP sample was investigated by Fe2+ and Cu2+ chelating activity, Trolox, ABTS, 1,1-diphenyl-2-picryl-hydrazil (DPPH) radical scavenging activity, and ferric reducing ability of plasma (FRAP) assay. MRPs derived from the glycine oligomer were found to be effective antioxidants in different antioxidant activity assays.

Effects of pH on Caramelization and Maillard Reaction Kinetics in Fructose‐Lysine Model Systems

ABSTRACT: The nonenzymatic browning reactions of fructose and fructose‐lysine aqueous model systems were investigated at 100 °C between pH 4.0 and pH 12.0 by measuring the loss of reactants and monitoring the pattern of UV‐absorbance and brown color development. At all the pH values tested, the loss of fructose was lower in the presence than in the absence of lysine. And, in lysine‐containing fructose solution, the sugar disappeared more rapidly than the amino acid. Lysine was moderately lost below pH 8.0. Caramelization of fructose, which accounted for more than 40% of total UV‐absorbance and 10 to 36% of brown color development, may therefore lead to overestimating the Maillard reaction in foods.

Relationship between thiol group modification and the binding site for fructose 2,6-bisphosphate on rabbit liver fructose-1,6-bisphosphatase.

A thiol group present in rabbit liver fructose-1,6-bisphosphatase is capable of reacting rapidly with N-ethylmaleimide (NEM) with a stoichiometry of one per monomer. Either fructose 1,6-bisphosphate or fructose 2,6-bisphosphate at 500 microM protected against the loss of fructose 2,6-bisphosphate inhibition potential when fructose-1,6-bisphosphatase was treated with NEM in the presence of AMP for up to 20 min. Fructose 2,6-bisphosphate proved more effective than fructose 1,6-bisphosphate when fructose-1,6-bisphosphatase was treated with NEM for 90-120 min. The NEM-modified enzyme exhibited a significant loss of catalytic activity. Fructose 2,6-bisphosphate was more effective than the substrate in protecting against the thiol group modification when the ligands are present with the enzyme and NEM. 100 microM fructose 2,6-bisphosphate, a level that should almost saturate the inhibitory binding site of the enzyme under our experimental conditions, affords only partial protection against the loss of activity of the enzyme caused by the NEM modification. In addition, the inhibition pattern for fructose 2,6-bisphosphate of the NEM-derivatized enzyme was found to be linear competitive, identical to the type of inhibition observed with the native enzyme. The KD for the modified enzyme was significantly greater than that of untreated fructose-1,6-bisphosphatase. Examination of space-filling models of the two bisphosphates suggest that they are very similar in conformation. On the basis of these observations, we suggest that fructose 1,6-bisphosphate and fructose 2,6-bisphosphate occupy overlapping sites within the active site domain of fructose-1,6-bisphosphatase. Fructose 2,6-bisphosphate affords better shielding against thiol-NEM modification than fructose 1,6-bisphosphate; however, the difference between the two ligands is quantitative rather than qualitative.

Fructose disposal and oxidation rates in the ovine fetus.

Fructose disposal and oxidation rates were measured in fetal lambs receiving a constant intravenous infusion of D-[U-14C]fructose. Approximately 60% of the infused tracer entered the placenta, but loss of fructose into the maternal circulation was negligible. Fructose was metabolized to lactate and CO2 in both the placenta and fetus, whereas there was no detectable conversion to glucose. In well-fed ewes the fetal disposal and utilization rates of fructose were 2.4 +/- 0.17 and 0.97 +/- 0.09 mg/min. kg, respectively. The umbilical excretion rate of CO2 originating from the oxidation of fetal fructose was 18.1 +/- 1.3 mumol/min. kg or 5.3% of total fetal CO2 production. This excretion rate is one-fifth of the CO2 excretion rate from fetal glucose carbon. In four ewes comparison of fructose metabolism in the fed and fasted states showed a significant decrease of fructose production and oxidation with fasting. Although fructose is present in high concentrations in the fetal blood of ungulates, its contribution to fetal oxidative metabolism is relatively small in comparison to glucose.

Limited proteolysis and photoaffinity labeling with 8-azido-ATP of fructose-6-phosphate,2-kinase and fructose-2,6-bisphosphatase.

Limited proteolysis and photoaffinity labeling of fructose-6-P,2-kinase and fructose-2,6-bisphosphatase were studied. Proteolysis by trypsin proceeds in two stages in which the first cleavage yields a product, Mr about 53,000, which has lost 90% of fructose-6-P,2-kinase, but retains nearly 80% of fructose-2,6-bisphosphatase. Further digestion of this product yields a second cleavage product, Mr about 50,000, which is completely devoid of the kinase and most of the phosphatase activities. These results indicate that fructose-6-P,2-kinase resides only in the original ("native") enzyme (Mr = 55,000), but fructose-2,6-bisphosphatase activity is present in both the native enzyme and the cleavage product(s). All three activities of fructose-6-P,2-kinase including the forward, the reverse, and ATP-ADP exchange activities are lost to the same degree by the mild proteolysis. Ki of fructose-6-P for fructose-2,6-bisphosphatase is not altered by the proteolysis. Partial protection against the proteolysis is provided by ATP, fructose-6-P, and fructose-2,6-P2. When the tryptic digestion of fructose-6-P,2-kinase:fructose-2,6-bisphosphatase was performed before and after phosphorylation of the enzyme by cAMP-dependent protein kinase, both the first and the second cleavage products contained the phosphorylation site. 8-Azido-ATP serves as a substrate for fructose-6-P,2-kinase with a Km of about 1 mM. Exposure of the enzyme-8-azido-ATP complex results in covalent incorporation (0.7 mol/mol of subunit) and 90% inactivation of fructose-6-P,2-kinase without loss of fructose 2,6-bisphosphatase. When the native and the first cleavage product of tryptic digestion were photoaffinity labeled with [alpha-32P]8-azido-ATP, the radiolabel occurred only in the native enzyme. These results provide evidence in support of, although not conclusive, the idea that the active sites of this bifunctional enzyme are different and located in two distinct sites.

Gamma irradiation of potatoes: Effects on sugar content, chip color, germination, greening, and susceptibility to mold

Russet Burbank potatoes that had been stored at 40°F. for 5 months after harvest were irradiated with 5,200 and 14,000 rad of Co60 gamma rays. In general, irradiation caused an accumulation of sugars. At 40°F., the sucrose level rose to nearly 3 times that of the control in 16 days following irradiation. Fructose and glucose showed smaller increases and the latter did not accumulate significantly in the tubers given the higher dose of gamma rays. At 70°F., the levels of sucrose and glucose in the irradiated tubers rose above those in the controls, the difference reaching a maximum in 4 days and then declining. Irradiation had no effect on loss of fructose at this temperature. Color of potato chips processed from the irradiated potatoes was in general darker than that of chips from control tubers. The storage-time pattern of color change resembled that of the reducing rather than total sugar. Fourteen thousand rad did not prevent initiation of germination in the tubers but did destroy their sprout-growth apparatus. Although the lower dosage did not prevent initiation and subsequent growth, it prevented the formation of secondary tubers, which appeared on the sprouted control tubers. Furthermore, unlike the controls, the low-dosage potatoes developed branching hair sprouts with no tendency toward apical dominance during the early stages of sprouting. The rate of greening of gamma-irradiated and illuminated tubers was significantly less than that of unirradiated illuminated controls. Evidence is presented that irradiation may increase the susceptibility of potatoes to attack by molds under some conditions.