Enzyme-assisted extraction of lycopene from tomato processing waste

A central composite design was used to optimize the enzyme-assisted extraction of lycopene from the peel fraction of tomato processing waste. Tomato skins were pretreated by a food-grade enzyme preparation with pectinolytic and cellulolytic activities and then subjected to hexane extraction. The factors investigated included extraction temperature (10–50 °C), pretreatment time (0.5–6.5 h), extraction time (0.5–4.5 h), enzyme solution-to-solid ratio (10–50 dm³/kg) and enzyme load (0–0.2 kg/kg). Overall, an 8- to 18-fold increase in lycopene recovery was observed compared to the untreated plant material. From a response surface analysis of the data, a second-degree polynomial equation was developed which provided the following optimal extraction conditions: T = 30 °C, extraction time = 3.18 h and enzyme load = 0.16 kg/kg. The obtained results strongly support the idea of using cell-wall degrading enzymes as an effective means for recovering lycopene from tomato waste.     

Lycopene recovery from tomato peel under mild conditions assisted by enzymatic pre-treatment and non-ionic surfactants

The tomato processing industry generates large quantities of tomato peel residues, usually creating environmental problems. These residues are a significant source of lycopene, thus providing an attractive alternative for profitable handling of these otherwise problematic by-products. The enzymatic pretreatment of these residues for lycopene recovery has already been employed, although the use of surfactants for enhancing the recovery has not been examined so far. The enzymatic pretreatment of tomato peels, using two commercially available pectinolytic enzyme preparations, was evaluated suggesting that there is an optimum pretreatment time of about 1 h, enzyme amount 250 Units/mL and no significant pH influence. Lycopene surfactant - assisted extraction was further investigated, showing that, among eight surfactants used, the most suitable was "Span 20", with an optimum ratio of 6-7 surfactant molecules per lycopene molecule. Sequential enzymatic pretreatment and surfactant-assisted extraction (30 min for each step) was evaluated leading to an improved lycopene extraction yield, with a somewhat smaller surfactant molar ratio (i.e. 4-5). In the latter case, the yield of lycopene recovery was almost four times greater compared to just 1 hr enzymatic pretreatment, and was approximately ten times greater compared to the recovery from untreated peels. Furthermore, such lipophilic compound recovery, avoiding the use of organic solvents, is environmentally attractive and ensures direct lycopene use in the food and cosmetics industries.     

Optimization of production and reaction conditions of polygalacturonase from Byssochlamys fulva

In the present study, the optimization of production and reaction conditions of polygalacturonase produced by a fungus Byssochlamys fulva MTCC 505 was achieved. The production of polygalacturonase with a considerable activity of 1.28 IU/ml was found when the culture was shaken at 30°C for 5 days in 100 ml of medium containing (w/v) 10 g/l pectin, 2 g/l NaNO?, 1 g/l KH?PO?, 0.5 g/l KCl, 0.5 g/l MgSO?. 7H?O, 0.001 g/l FeSO?. 7H?O, 0.001 g/l CaCl?. The best carbon and nitrogen source for this enzyme were pectin (1%) and Ca(NO?)? (0.1%), respectively. The enzyme gave maximum activity at incubation time of 72 h, temperature of 30°C and pH 4.5. During the optimization of reaction conditions, the enzyme showed maximum activity in sodium citrate buffer (50 mM) of pH 5.5 at 50°C reaction temperature for 15 minutes of incubation. The enzyme showed greater affinity for polygalacturonic acid as substrate (0.5%). Km and Vmax values were 0.15 mg/ml and 4.58 μmol/ml/min. The effect of various phenolics, thiols, protein inhibitors and metal ions on the enzyme activity was investigated. The enzyme was quite stable at 4°C and 30°C. At 40°C the half life of the enzyme was 6 h and at 60°C it was 2 h.     

Synthesis and thermal characterization of xylan-graft-polyacrylonitrile

In this study emulsion polymerization of acrylonitrile using xylan from agricultural waste material (corn cob) and cerium ammonium nitrate was investigated in terms of catalyst acid. Stock ceric solutions were prepared using either nitric or perchloric acid as catalyst. Optimum conditions were determined using different parameters such as reaction time, temperature, and component concentrations. Nitric acid catalyzed reactions resulted in maximum conversion ratio (96%) at 50°C, 1h where ceric ion, acrylonitrile, xylan, and catalyst concentrations were 21.7mmoll(-1), 0.5moll(-1), 0.2% (w/v), and 0.1moll(-1), respectively. However, 83% conversion was obtained with perchloric acid catalysis at 27°C, 1h where concentrations were 5.4mmoll(-1), 0.8moll(-1), 0.5% (w/v), and 0.2moll(-1), respectively. Copolymer synthesis using perchloric acid was realized at milder conditions than using nitric acid. Thermal analyses of obtained polymers were conducted to characterize copolymers. Results showed that calculated activation energy, maximum degradation temperature, and heat of thermal decomposition changed relying mainly on molecular weight.     

Preparation and evaluation of antioxidant peptides from ethanol-soluble proteins hydrolysate of Sphyrna lewini muscle

To get high yield of ethanol-soluble proteins (EP) and the antioxidant peptides from Sphyrna lewini muscle, orthogonal experiments (L(9)(3)(4)) were applied to optimize the best extraction conditions and enzyme hydrolysis conditions. The yield of EP reached 5.903±0.053% under the optimum conditions of ethanol concentration 90%, solvent to material ratio 20:1, extraction temperature of 40°C and extraction time of 80min. The antioxidant SEPH (EP hydrolysate of S. lewini muscle) was prepared by using papain under the optimum conditions of enzymolysis time 2h, total enzyme dose 1.2%, enzymolysis temperature 50°C and pH 6, and its DPPH radical scavenging activity reached 21.76±0.42% at the concentration of 10mg/ml. Two peptides (F42-3 and F42-5) were isolated from SEPH by using ultrafiltration, anion-exchange chromatography, gel filtration chromatography and RP-HPLC. The structures of F42-3 and F42-5 were identified as Trp-Asp-Arg and Pro-Tyr-Phe-Asn-Lys with molecular weights of 475.50Da and 667.77Da, respectively. F42-3 and F42-5 exhibited good scavenging activity on hydroxyl radical (EC(50) 0.15mg/ml and 0.24mg/ml), ABTS radical (EC(50) 0.34mg/ml and 0.12mg/ml), and superoxide anion radical (EC(50) 0.09mg/ml and 0.11mg/ml), but moderate DPPH radical (EC(50) 3.63mg/ml and 4.11mg/ml). F42-3 and F42-5 were also effectively against lipid peroxidation in the model system and peroxyl free radical scavenging in β-carotene linoleic acid assay. Their high activities were due to the smaller size and the presence of antioxidative amino acids within the peptide sequences.     

Biorefinery cascade processing for creating added value on tomato industrial by-products from Tunisia

Background

In today’s consumer perception of industrial processes and food production, aspects like food quality, human health, environmental safety, and energy security have become the keywords. Therefore, much effort has been extended toward adding value to biowastes of agri-food industries through biorefinery processing approaches. This study focused, for the first time, on the valorization of tomato by-products of a Tunisian industry for the recovery of value-added compounds using biorefinery cascade processing.

Results

The process integrated supercritical CO₂ extraction of carotenoids within the oil fractions from tomato seeds (TS) and tomato peels (TP), followed by a batch isolation of protein from the residues. The remaining lignocellulosic matter from both fractions was then submitted to a liquid hot water (LHW) hydrolysis. Supercritical CO₂ experiments extracted 5.79% oleoresin, 410.53 mg lycopene/kg, and 31.38 mg β-carotene/kg from TP and 26.29% oil, 27.84 mg lycopene/kg, and 5.25 mg β-carotene/kg from TS, on dry weights. Protein extraction yields, nearing 30% of the initial protein contents equal to 13.28% in TP and 39.26% in TS, revealed that TP and TS are a rich source of essential amino acids. LHW treatment run at 120–200 °C, 50 bar for 30 min showed that a temperature of 160 °C was the most convenient for cellulose and hemicellulose hydrolysis from TP and TS, while keeping the degradation products low.

Conclusions

Results indicated that tomato by-products are not only a green source of lycopene-rich oleoresin and tomato seed oil (TSO) and of protein with good nutritional quality but also a source of lignocellulosic matter with potential for bioethanol production. This study would provide an important reference for the concept and the feasibility of the cascade fractionation of valuable compounds from tomato industrial by-products.

Open image in new window

Graphical abstract Schema of biorefinery cascade processing of tomato industrial by-products toward isolation of valuable fractions.

     

番茄红素提取工艺的优化

通过研究预处理方法、有机溶剂及混合溶剂、温度、时间和固液比等因素对分离番茄红素的影响,探索最优化工艺,为工业化高效提取提供依据.实验结果表明:优化温度55℃,温浴番茄果皮浆状物2.5 h后,经离心、乙醇洗涤,再按照固液比为1:4(g/mL),用V(石油醚):V(丙酮)为1:2的混合溶剂在封口容器中,于50℃水浴中萃取番茄红素25 min,期间不断轻微摇晃以确保萃取充分.用此法提取番茄红素成本低、效率高、易于自动化,具有广阔的工业化应用前景.     

The antioxidant and anti-inflammatory properties of lycopene in mice lungs exposed to cigarette smoke

Lycopene is a carotenoid with known antioxidant and anti-inflammatory properties. We aimed to evaluate the in vitro and in vivo effects of lycopene on reducing the redox imbalance and inflammation induced by cigarette smoke (CS). For the in vitro study, J774A.1 (macrophages) cells were incubated in the presence of 0.5, 1.0, 2.0, 4.0, 8.0, 10.0 and 25 μM of lycopene for 3, 6 and 24 h or in the presence of 0.1%, 0.25%, 0.5%, 0.625%, 1.25%, 2.25%, 5% and 10% cigarette smoke extract (CSE) for 3, 6 and 24 h to assess cell viability and measurement of intracellular reactive oxygen species (ROS). For the in vivo study, 40 mice were divided into 5 groups: a control exposed to ambient air (CG), a vehicle-control group that received 200 μl of sunflower oil by orogastric gavage, a group exposed to CS and two groups administered lycopene (diluted in sunflower oil) at doses of either 25 or 50 mg/kg/day prior to exposure to CS (LY25+CS and LY50+CS). The total treatment time lasted 5 days. A cell viability decrease was observed at 10- and 25-μM concentrations of lycopene in 3, 6 and 24 h compared with CG. There was an increase of ROS production in 24 h in CS compared with CG. Lycopene concentrations of 1 μM and 2 μM were able to reduce the production of ROS in 24 h compared with CS. In the bronchoalveolar lavage fluid, the total number of leukocytes increased in the CS group compared with the control groups (CG). Administration with lycopene at the highest dose suppressed this CS-induced increase in leukocytes. Lipid peroxidation and DNA damage increased in the CS group compared with that in the controls, and this increase was suppressed by lycopene at the highest dose. In contrast, superoxide dismutase activity decreased in the CS group compared with that in the controls. Catalase activity also increased in the CS group compared with that in both control groups, and this increase was suppressed in LY25+CS and LY50+CS. There was an increase in the levels of tumor necrosis factor-α, interferon-γ and interleukin-10 after exposure to CS, and these effects were suppressed by both doses of lycopene. These data elucidate the role of lycopene as an antioxidant and anti-inflammatory agent in these two models of short-term exposure to CS.     

Dilute-sulfuric acid pretreatment of cattails for cellulose conversion

The use of aquatic plant cattails to produce biofuel will add value to land and reduce emissions of greenhouse gases by replacing petroleum products. Dilute-sulfuric acid pretreatment of cattails was studied using a Dionex accelerated solvent extractor (ASE) varying acid concentration (0.1-1%), treatment temperature (140-180 °C), and residence time (5-10 min). The highest total glucose yield for both the pretreatment and enzyme hydrolysis stages (97.1% of the cellulose) was reached at a temperature of 180 °C, a sulfuric acid concentration of 0.5%, and a time of 5 min. Cattails pretreated with 0.5% sulfuric acid are digestible with similar results at enzyme loadings above 15 FPU/g glucan. Glucose from cattails cellulose can be efficiently fermented to ethanol with an approximately 90% of the theoretical yield. The results in this study indicate that cattails are a promising source of feedstock for advanced renewable fuel production.     

The effect of hyperthermia on micronucleus induction by mutagens in mice

We administered mitomycin C (0.5 mg/kg) intraperitoneally to hyperthermic-treated mice and examined the effect of hyperthermia on micronucleus induction. Hyperthermia enhanced micronucleus induction. The timing of chemical administration relative to the start of hyperthermic treatment (37 degrees C ambient temperature) influenced micronucleus frequency, and the effect was greatest 2 h after the start of hyperthermic treatment. But the hyperthermic treatment did not change the time course of micronucleus induction. In addition, we investigated the effect of hyperthermia on micronucleus induction by chemicals with different modes of action, i.e., alkylating agents (mitomycin C at 0.1-0.5 mg/kg, cyclophosphamide at 1.25-10 mg/kg), a spindle poison (colchicine at 0.05-1.0 mg/kg), and an antimetabolite (5-fluorouracil at 2.5-50 mg/kg). Hyperthermia enhanced only the clastogenicity of alkylating agents.     

Development of a liquid chromatography-tandem mass spectrometry with pressurized liquid extraction for determination of glucocorticoid residues in edible tissues

A multi-residues method using pressurized liquid extraction (PLE) and liquid chromatography combined with mass spectrometry (LC-MS/MS) has been developed for determination of eight glucocorticoids (prednisone, prednisolone, hydrocortisone, methylprednisolone, dexamethasone, betamethasone, beclomethasone, fludrocortisone) in muscle of swine, cattle, and sheep. Parameters affecting PLE extraction including extraction solvent, extraction temperature, extraction pressure and extraction cycles were optimized. The optimized method employed 11 ml extraction cells, hexane-ethyl acetate (50:50, v/v) as extraction solvent, 1500 psi of extraction pressure and 50°C of extraction temperature. The samples were detected by LC-ESI-MS/MS in negative mode with selected reaction monitoring (SRM) mode. The recovery of glucocorticoids spiked at levels of 0.5-6 μg kg(-1) ranged from 70.1% to 103.1%; the between-day relative standard deviations were no more than 9.6%. The limits of quantification were 0.5-2 μg kg(-1) in muscle. The results demonstrated that the method is simple, fast, robust, and suitable for identification and quantification of glucocorticoids residues in foods of animal origin.     

Factors influencing lycopene content of foods, and lycopene intake of Hungarian population

Lycopene is an acyclic, biologically active carotenoid that constitutes foods, its preventive role in several cancerous diseases have been proved by epidemiological and experimental data. Its beneficial role in maintenance of human health is related to its significant antioxidant properties. Data of dietary lycopene intake of the Hungarian population is not available. The aims of the present complex study were 1) to measure the lycopene content of foods frequently consumed in Hungary, 2) to investigate the effect of agrotechnological procedures and food processing on lycopene content of tomatoes, 3) to estimate the lycopene intake in two groups of the Hungarian population with the use of a three-day dietary record. The best lycopene sources are the raw (5.0-16.0 mg/100 g) and processed tomatoes and tomato products (3.0-80.0 mg/100 g), and also watermelon (3.6-6.2 mg/100 g). The variety of the plants, the growing circumstances, and the weather conditions significantly influence the lycopene content of freshly consumed and processed tomato fruits. Mild technological processes can preserve a considerable amount of the original lycopene content in tomato. The estimated average dietary intakes of the Hungarian children (n=521) and adults (n=205) were 2.98 +/- 4.71 mg/day/capita, and 4.24 +/- 8.47 mg/day/capita, respectively. Optimal climate conditions of Hungary makes possible to produce tomato fruits with high dietary value including significant amount of health protective lycopene. Increased consumption of tomato and tomato products with high concentration of lycopene may improve the antioxidant capacity of human body, and the risk of several cancerous diseases may be reduced.     

Purification and biochemical characterization of extracellular laccase from the ascomycete Paraconiothyrium variabile

An extracellular laccase-producing ascomycete was isolated from soil and identified as Paraconiothyrium variabile using rDNA sequence analysis. Typical laccase substrates including 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS), 2,6-dimethoxyphenol (DMP), and guaiacol were oxidized by the purified enzyme (designated as PvL). The molecular mass of PvL was 84 kDa and it showed a pI value of 4.2. The enzyme acted optimally at pH 4.8 and exhibited an optimum temperature of 50 °C. Using ABTS, PvL represented Km and Vmax of 203 μM and 40 μmol min(-1) mg(-1), respectively. After 24 h incubation at pH 4.8 and 4 °C, 80% of the initial activity of PvL remained. The enzyme was inhibited by Fe2+, Hg2+, and Mn2+, but induced by Cu2+. EDTA (10 mM), 1,4-dithiothreitol (DTT) (0.1 mM), and NaN3 (10 mM) were found to completely inhibit PvL. Sixty-eight percent of Malachite green was decolorized by 4 U/mL of PvL after 15 min incubation at 30 °C.     

Influence of induction conditions on the expression of carbazole dioxygenase components (CarAa, CarAc, and CarAd) from Pseudomonas stutzeri in recombinant Escherichia coli using experimental design

Carbazole 1,9a-dioxygenase (CarA), the first enzyme in the carbazole degradation pathway used by Pseudomonas sp., was expressed in E. coli under different conditions defined by experimental design. This enzyme depends on the coexistence of three components containing [2Fe-2S] clusters: CarAa, CarAc, and CarAd. The catalytic site is present in CarAa. The genes corresponding to components of carbazole 1,9a-dioxygenase from P. stutzeri were cloned and expressed by salt induction in E. coli BL21-SI (a host that allows the enhancement of overexpressed proteins in the soluble fraction), using the vector pDEST?14. The expression of these proteins was performed under different induction conditions (cell concentration, temperature, and time), with the help of two-level factorial design. Cell concentration at induction (measured by absorbance at 600 nm) was tested at 0.5 and 0.8. After salt induction, expression was performed at 30 and 37°C, for 4 h and 24 h. Protein expression was evaluated by densitometry analysis. Expression of CarAa was enhanced by induction at a lower cell concentration and temperature and over a longer time, according to the analysis of the experimental design results. The results were validated at Abs (ind) = 0.3, 25°C, and 24 h, at which CarAa expression was three times higher than under the standard condition. The behavior of CarAc and CarAd was the inverse, with the best co-expression condition tested being the standard one (Abs (ind) = 0.5, T = 37°C, and t = 4 h). The functionality of the proteins expressed in E. coli was confirmed by the degradation of 20 ppm carbazole.     

Rat liver alcohol dehydrogenase. I. Purification and characterization

Alcohol dehydrogenase was purified in 14 h from male Fischer-344 rat livers by differential centrifugation, (NH4)2SO4 precipitation, and chromatography over DEAE-Affi-Gel Blue, Affi-Gel Blue, and AMP-agarose. Following HPLC more than 240-fold purification was obtained. Under denaturing conditions, the enzyme migrated as a single protein band (Mr congruent to 40,000) on 10% sodium dodecyl sulfate-polyacrylamide gels. Under nondenaturing conditions, the protein eluted from an HPLC I-125 column as a symmetrical peak with a constant enzyme specific activity. When examined by analytical isoelectric focusing, two protein and two enzyme activity bands comigrated closely together (broad band) between pH 8.8 and 8.9. The pure enzyme showed pH optima for activity between 8.3 and 8.8 in buffers of 0.5 M Tris-HCl, 50 mM 2-(N-cyclohexylamino)ethanesulfonic acid (CHES), and 50 mM 3-(cyclohexylamino)-1-propanesulfonic acid (CAPS), and above pH 9.0 in 50 mM glycyl-glycine. Kinetic studies with the pure enzyme, in 0.5 M Tris-HCl under varying pH conditions, revealed three characteristic ionization constants for activity: 7.4 (pK1); 8.0-8.1 (pK2), and 9.1 (pK3). The latter two probably represent functional groups in the free enzyme; pK1 may represent a functional group in the enzyme-NAD+ complex. Pure enzyme also was used to determine kinetic constants at 37 degrees C in 0.5 M Tris-HCl buffer, pH 7.4 (I = 0.2). The values obtained were Vmax = 2.21 microM/min/mg enzyme, Km for ethanol = 0.156 mM, Km for NAD+ = 0.176 mM, and a dissociation constant for NAD+ = 0.306 mM. These values were used to extrapolate the forward rate of ethanol oxidation by alcohol dehydrogenase in vivo. At pH 7.4 and 10 mM ethanol, the rate was calculated to be 2.4 microM/min/g liver.     

Tolerance of the widespread cyanobacterium Nostoc commune to extreme temperature variations (?269 to 105°C), pH and salt stress

Nostoc commune is a widespread colonial cyanobacterium living on bare soils that alternate between frost and thaw, drought and inundation and very low and high temperatures. We collected N. commune from alternating wet and dry limestone pavements in Sweden and tested its photosynthesis and respiration at 20°C after exposure to variations in temperature (-269 to 105°C), pH (2-10) and NaCl (0.02-50 g NaCl kg(-1)). We found that dry field samples and rewetted specimens tolerated exposure beyond that experienced in natural environmental conditions: -269 to 70°C, pH 3-10 and 0-20 g NaCl kg(-1), with only a modest reduction of respiration, photosynthesis and active carbon uptake at 20°C. (14)CO(2) uptake from air declined markedly below zero and above 55°C, but remained positive. Specimens maintained a high metabolism with daily exposure to 6 h of rehydration and 18 h of desiccation at -18 and 20°C, but died at 40°C. The field temperature never exceeded the critical 40°C threshold during the wet periods, but it frequently exceeded this temperature during dry periods when N. commune is already dry and unaffected. We conclude that N. commune has an excellent tolerance to low temperatures, long-term desiccation and recurring cycles of desiccation and rewetting. These traits explain why it is the pioneer species in extremely harsh, nutrient-poor and alternating wet and dry environments.     

Purification and properties of rat kidney catechol-O-methyltransferase]

The S-adenosyl-methionine: catechol-O-methyltransferase (EC 2.1.1.6) from rat kidney was purified about 650 fold as compared with the homogenate and the result of disc electrophoresis presented. The purification involved extraction, precipitation at pH 5, ammonium sulfate fractionation, Chromatographies on Biogel 0.5 m, Ultrogel AcA 44 and DE Sephadex A 50. Affinity chromatography was tried but unsuccessful. The enzyme exhibited two pH optima at 7.9 and 9.6 with a minimum at about 8.9. The COMT had a temperature optimum of 50 degrees C, with activation energy of 23.1 Kcal/Mole between 25-35 degrees C, 18.9 Kcal/mole between 35-45 degrees C and the Q10 within the range of 25-35 degrees amounted to 3.5. The molecular weight was estimated to be 21500+/-1000 daltons from its behavior on Ultrogel AcA 44 and the pH1 determined by electrofocalisation was near 5.50. The time of half life of the best purified enzymatic extract was found to be 2 h 10 min. at -20 degrees C. At basic pH the instability of the enzyme was increased. Since O-methylation required the presence of divalent cations, our results show that apparent Michaelis constants for Mg++ and Mn++ were respectively 0.50 X 10(-3) M and 0.33 X 10(-5) M. The study of their Hill's number indicated that there was only one point of fixation on the enzyme. The Km value determined by Florini and Vestling's method were 2.5 X 10(-4) M and 11.9 X 10(-5) M for epinephrine and S-adenosyl-methionine respectively. All results were discussed with respect to other investigations.     

Integrating low water potential seed hydration with other treatments to improve cold tolerance

Matriconditioning improved the performance of pepper, tomato, sweet corn, snap bean, table beet, sugar beet and watermelon seeds in early field plantings at suboptimal temperatures (averaged over 10 d after planting) ranging from 12 to 18 °C. Reduction in the time to 50% (T(50)) emergence in conditioned seeds ranged from 0·6 d in watermelon to 3·3 d in pepper and improvement in emergence from 10% in sugar beet to 30% in table beet. Further improvement in emergence occurred by inclusion of pesticides and/or gibberellin during conditioning. A 4 d conditioning of pepper at 25 °C was superior to 7 d conditioning at 15 °C in seeds germinated at 15 °C on filter paper, but 15 °C conditioning was superior in improving percentage emergence in early field plantings. Tomato seeds conditioned at 15 or 25 °C performed equally well in the field. A 2 d conditioning was superior to 1 d conditioning in improving the performance of supersweet sweet corn cultivars grown in a growth chamber at 10/20 °C. The water uptake rate in the presence of Micro-Cel E during matriconditioning of sweet corn seeds was slower than when the seeds were exposed to the same amount of water in absence of the carrier. Electrolyte leakage was greater in supersweet 'Challenger' sweet corn seeds carrying the sh(2) gene compared to the sugary type sweet corn 'More', and in both cases matriconditioning reduced the leakage. Lettuce seeds matriconditioned for 24 h had higher 1-aminocyclopropane-l-carboxylic acid (ACC) content, developed greater ACC oxidase activity and performed better at 10 °C (germinated earlier and had higher percentage germination) than the untreated seeds. Matriconditioning appears to bring about beneficial physical, physiological and biochemical changes that seemingly improve embryo growth potential and tolerance to low temperatures.     

Bioavailability of synthetic and biosynthetic deuterated lycopene in humans

Current knowledge of the bioavailability of lycopene in humans is limited due to the inability to distinguish newly administered lycopene from the body reserves of lycopene. A quantitative method to assess the absorption and relative bioavailability of newly absorbed synthetic or natural lycopene was developed using two deuterated lycopene sources, in conjunction with an advanced LC/APCI-MS (liquid chromatography/atmospheric pressure chemical ionization-mass spectrometry) to analyze newly absorbed lycopene in blood samples of study subjects. Two subjects (1 male and 1 female) consumed hydroponically grown tomatoes containing deuterium-enriched lycopene (80-84 g wet weight tomato containing 16.3 and 17.4 micromol lycopene, respectively) and two subjects (1 male, and 1 female) consumed 11 micromol synthetic (2)H(10) lycopene in 6 g of corn oil. Tomatoes were steamed and pureed. The doses were given together with a liquid formulated drink with 25% energy from fat. Our results showed that up to 34 days after taking an oral (2)H(10) lycopene dose (synthetic or from tomato) with a liquid formula drink, the area under the curve of the average serum percent enrichment response of synthetic lycopene reached 33.9 (+/-1.7) nmol-day/micromol lycopene in the dose, whereas that of lycopene from the tomato dose was 11.8 (+/-0.3) nmol-day/mumol lycopene in the dose. Our study provides evidence that the absorption of physiological levels of lycopene in intrinsically labeled tomatoes can be studied in humans. From these preliminary investigations, we find that the bioavailability of synthetic lycopene in oil appears to be about three times higher than that of lycopene from steamed and pureed tomatoes.     

Extraction conditions affecting supercritical fluid extraction (SFE) of lycopene from watermelon

Lycopene, a carotenoid linked to protection against certain forms of cancer, is found in produce such as papaya, red-fleshed tomatoes, grapefruit and watermelon. The preparation of a supercritical CO2 (SC-CO2) watermelon-lycopene extract could serve as a food grade source of this carotenoid. This study established preliminary conditions for enhancing SC-CO2 extraction of lycopene from watermelon. Freeze-dried watermelon was extracted with SC-CO2 and ethanol as an organic co-solvent. The lycopene concentration was determined by HPLC, with absorbance measured at 503 nm. In an initial set of experiments, the effects of extraction temperature (70-90 degrees C), pressure (20.7-41.4 MPa) and co-solvent ethanol addition (10-15%) were evaluated. A lycopene yield of 38 microg per gram of wet weight was obtained at 70 degrees C, 20.7 MPa, and 15% by volume ethanol. The extraction of fresh (non-freeze-dried) watermelon yielded 103+/-6 microg lycopene per gram fresh fruit weight. Of the parameters tested, temperature had the most effect on lycopene yield. Thus, in another set of experiments, the temperature was varied from 60-75 degrees C at an extraction pressure of 20.7 MPa in the presence of 15% ethanol. Studies showed that freeze-dried watermelon flesh loses lycopene in storage. In accounting for lycopene storage losses, lycopene yields at 60 degrees C extraction temperature were 14% greater than those obtained at 70 degrees C.