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Mandarin orange (Citrus reticulata) juice was packed in two different non-transparent cartons made of polyethylene, cardboard and (1) aluminum foil (Tetrapak® ) or (2) ethylene vinyl alcohol copolymers (Pure-pak® ) and was stored at 4C or room temperature (25 ± 3C). During the shelf life of these juices (35 days), changes in the headspace gas composition, vitamin C and CIEL*a*b* color coordinates were evaluated. In addition, a consumer panel evaluated the sensory color of the juices. Mandarin orange juices darkened and ascorbic acid content decreased with storage time. Type of carton and storage temperature played a predominant role in determining the final juice quality, with Tetrapak® carton providing the juice with the best quality (intense orange color and high vitamin C content and consumer preference) throughout their shelf life. PRACTICAL APPLICATIONS This study was a clear example of how research can help real food companies in selecting the right materials for their production lines. In this particular case, the results presented show how Tetrapak® packaging led to a final mandarin orange juice of higher quality compared to Pure-pak® packaging. Therefore, citrus processing companies have some scientific data comparing the behavior of these two types of non-transparent cartons. Besides, the companies manufacturing these cartons also have some information about their materials and can use it to improve them. [ABSTRACT FROM AUTHOR]

Eight mandarin cultivars have been analyzed for their content of vitamin C, minerals (Ca, Mg, K, Na, Fe, Cu, Mn, and Zn), CIELab color coordinates (L*, a*, b*, C*, and hab), total volatile compounds content and sensory aroma intensity of juice. Experimental results proved that no important enough differences were found in the minerals contents to decide which mandarin cultivar was of higher quality. Clemenules provided the darkest juice with the highest vitamin C content and with the most intense mandarin aroma. On the other hand, Nova and Hernandina mandarin could be considered as the worst cultivars for juice production. Finally if Clemenules mandarins were not available for juice processing, Orogrande, Clemenpons, Ellendale, and Marisol could also be good options. [ABSTRACT FROM AUTHOR]

Lipoxygenase (LOX) from eggplant (Solanum melongena L. cv. Belleza negra) was partially purified, and the products and kinetics of the enzyme were studied. Linoleic acid (LA) was the best substrate for this enzyme. Product analysis by HPLC and GC/MS revealed that, at its pH optimum (pH 7.0), the enzyme converted LA almost totally into the 9-hydroperoxy isomer, whereas the 13-hydroperoxy isomer was only a minor product. At this pH, the enzyme had K(m) and V(max) values for LA of 1.4 microM and 2.2 micromol min(-1) (mg of protein)(-1), respectively, when the monomeric form of LA was used as substrate. The dependence of eggplant LOX activity on the physicochemical properties of LA was also studied. Experiments revealed that LA aggregates were used more efficiently than monomeric LA as substrate. The apparent substrate cooperativity observed may be due to the different activities exhibited toward monomers and aggregates. This result can be interpreted as a substrate-aggregation dependent activity.

When the effect of calcium on the oxidation of linoleic acid by potato tuber 5-lipoxygenase (LOX) was investigated, it was seen to promote the enzyme's activity at pH values higher than the optimum pH of 6.3, resulting in an enzyme activation at alkaline pH. Kinetic analysis of calcium activation at different pH values revealed that the cation abolished the inhibition by high substrate concentration, which occurs in the absence of Ca(2+), thus leading to activation at high substrate concentration. Studies were conducted to investigate the influence of Ca(2+) on the physicochemical nature of the substrate and its effect on the LOX activity expression. It was concluded that the aggregation mode rather than the aggregation state of linoleic acid is responsible for potato 5-LOX changes.

A new reversed-phase high-performance liquid chromatography method for the separation of regioisomeric products from lipoxygenase acting on linoleic acid was studied. The addition of salts to the mobile phase improved the retention and separation behaviour of 13-hydroperoxy-9,11-octadecadienoic acid and 9-hydroperoxy-10,12-octadecadienoic acid with respect to the results obtained with other mobile phases reported in the literature. The effect of the pH and ionic strength of the buffer on the retention times, capacity factor and separation factor of these lipoxygenase products were also studied. The pH optimum coincided with the pKa of linoleic acid (close to 7 depending on the fatty acid concentration). Phosphate concentrations close to 100 mM considerably reduced the retention times and led to better separation of the mixture of both products. Finally, this method was applied to the identification and separation of two linoleic acid hydroxides (13-hydroxy-9,11-octadecadienoic acid and 9-hydroxy-10,12-octadecadienoic acid) obtained by the reduction of their corresponding hydroperoxides.

The capability of cyclodextrins (CDs) to greatly enhance the solubility in water of poorly water-soluble substances makes them an ideal alternative system for studying the expression of enzyme activity with such substrates in aqueous solution. In order to evaluate the behaviour of the enzymes in presence of CDs a study of the lipoxygenase (LOX)-catalyzed oxidation of polyunsaturated fatty acids (PUFA) as model reaction has been carried out. This was done by using LOX from two different sources (soybean and potato tuber), at two pH values (6.3 and 9.0), with two substrates (linoleic acid and arachidonic acid) and three types of CD (beta-CD, methyl-beta-CD and monoglucosyl-beta-CD). PUFA have been shown to form inclusion complexes of 1:2 stoichiometry which are in equilibrium with free PUFA and free CD, thus complexation is governed by two equilibrium constants, K1 and K2 (J.M. López-Nicolás et al., Biochem. J. 308 (1995) 151-154; R. Bru et al., Colloids Surf. 97 (1995) 263-269). For the oxidation of PUFA by LOX in the presence of beta-CD we propose a model in which free PUFA is the only effective substrate, thus the oxidation of the complexed substrate requires the previous dissociation of the complex. The equilibrium constants of complex formation are determined by both a physico-chemical and an enzymatic method. In spite of giving quite similar results, the second was proven to be more accurate so it was employed in further studies. CD was shown to slow down the reaction rate of LOX, specifically due to the increase of Km, Vmax remaining unchanged. That apparent inhibition is due to removal of effective (free) substrate in the form of inclusion complexes. This 'sequestered' substrate can, however, be converted since it is in equilibrium with the free. The feasibility of realizing a CD-mediated accurate control over the conversion rate is demonstrated in the experiment called 'cyclodextrin assay' in which the concentration of the free substrate is calculated by using the equilibrium constants of complex formation and setting the initial concentrations of total substrate and total CD. From the observation of the reaction progress curves in the conditions of the CD assay, we have studied some characteristic parameters of the oxidation of PUFA by LOX in this new medium, such as enzymatic activity, duration of linear product accumulation and the lag phase.

Using the detergent octaethylene glycol monododecyl ether (C12E8), a spectrophotometric mixed micellar assay for lipoxygenas (LOX) activity was designed. Potato LOX was able to use the linoleic acid (LA) solubilized in C12E8 micelles, displaying the characteristic induction period of LOX-catalyzed LA peroxidation. In the mixed micellar system, LOX responds to the LA surface concentration expressed as mol% (=[lipid]*100/([detergent]-cmc)) and not to the molarity of the LA. For both potato and soybean LOX, Vmax was independent of the mixed micelle concentration, while Km was independent as well when expressed as mol% but was dependent on C12E8 concentration when expressed in molar. In mixed micelles, H2O2 shortened the induction period, while 13-hydroperoxylinoleic acid and t-butyl hydroperoxide completely removed it. C12E8/LA proved to be a reliable system for assaying LOX activity at pH values around neutrality. Like Tween 20, this system avoided the turbidity problems arising from the protonated fatty acid and did not interfere with the uv-absorption band of the hydroperoxide product. However, this system is superior to the commonly used Tween 20 because it permits investigation of the lipid requirements of LOX since the concentration-independent Km can be determined both in mol% and as the absolute number of lipids per micelle. In addition, the detergent did not affect the enzyme through any side effects.