Development of antioxidant food packaging materials with controlled release properties

In this study, cellulose acetate (CA) films with different morphological features were prepared in order to control the release rates of low molecular weight natural antioxidants, L-ascorbic acid and L-tyrosine. Increasing CA content in the casting solution decreased the average pore size and porosity of the films, thus, reduced the diffusion rates of both antioxidants through the films. Although both antioxidants have similar molecular weights, L-tyrosine released into water much more slowly than L-ascorbic acid. The highest antioxidant activity in release test solutions was observed with highly porous L-tyrosine containing films. However, when the porosity of the films reduced, the antioxidant activity of L-ascorbic acid released into solution was found to be higher due to trapping of significant amount of L-tyrosine in dense films. The use of different antioxidants caused different changes in morphological and mechanical properties of the CA films. Varying the structural features of the films with the preparation conditions or using different surfaces of the films allowed the controlled release of each antioxidant.     

Thermal inactivation kinetics of peroxidase and lipoxygenase from fresh pinto beans (Phaseolus vulgaris)

 Thermal inactivation kinetics of crude peroxidase (POX) and lipoxygenase (LOX) in fresh pinto beans were studied over the temperature range of 55–90°C. The inactivation of both enzymes followed first-order kinetics. The biphasic inactivation curves for POX indicate the existence of several isoenzymes of varying heat stability. In the temperature range of 55–70°C, the activation energies (E _a) of POX were 46.5 kcal·mol^–1 for the heat-labile portion and 37.6 kcal·mol^–1 for the heat-stable portion. On the other hand, the LOX enzyme had an E _a value of 42.26 kcal·mol^–1 at 55–75°C and 49.1 kcal·mol^–1 at 55–90°C. Received: 28 July 1997 / Revised version: 16 October 1997     

Antioxidant activity of protein extracts from heat-treated or thermally processed chickpeas and white beans

In this study, antioxidant activities of water-soluble protein extracts from chickpeas and white beans were investigated. The area under the curve (AUC) values of lyophilized crude protein extracts (dialyzed or undialyzed) from thermally processed (121 °C for 20 min) or heat-treated (90 °C for 20 min) chickpeas (73–91 μmol trolox/g) and white beans (39–67 μmol trolox/g) indicated a higher free radical-scavenging capacity and thermostability for chickpea proteins than for white bean proteins. The thermal processing also increased the Fe⁺²-chelating capacity of lyophilized chickpea crude protein extracts 1.8-fold whereas it caused a 2.3-fold reduction in the Fe⁺²-chelating capacity of lyophilized white bean crude protein extracts. Dialysis increased the protein content of lyophilized chickpea extracts 1.5–2-fold but it did not affect the protein content of lyophilized white bean extracts significantly. Ammonium sulfate precipitation was not effective for selective precipitation of antioxidant proteins. However, it improved the free radical-scavenging capacity of lyophilized protein extracts from thermally processed chickpeas and white beans by almost 25% and 100%, respectively. DEAE-cellulose chromatography, indicated the presence of five (A₁–A₅) and three (B₁–B₃) antioxidant protein fractions in heat-treated and thermally processed chickpea protein extracts, respectively, and can be used for the partial purification of antioxidant proteins. The results of this study showed the good potential of chickpea proteins as thermostable natural food antioxidants.     

Active packaging of ground beef patties by edible zein films incorporated with partially purified lysozyme and Na2EDTA

In this study, antimicrobial activity of zein films incorporated with partially purified lysozyme and disodium ethylenediaminetetraacetic acid (Na₂EDTA) has been tested on selected pathogenic bacteria and refrigerated ground beef patties. The developed films containing 700 μg cm^?2 lysozyme and 300 μg cm^?2 Na₂EDTA showed antimicrobial activity on Listeria monocytogenes, Escherichia coli O157:H7, and Salmonella typhimurium. The application of lysozyme and Na₂EDTA incorporated zein films on beef patties significantly decreased total viable counts (TVC) and total coliform counts after 5 days of storage compared to those of control patties (P < 0.05). Zein films incorporated with lysozyme and Na₂EDTA or Na₂EDTA alone significantly slowed down the oxidative changes in patties during storage (P < 0.05). Redness indices of patties coated with zein films were significantly lower than those of uncoated control patties during storage (P < 0.05). This study demonstrated the potential usage of zein films containing lysozyme and Na₂EDTA for active packaging of refrigerated meat products.     

Development of pectin–eugenol emulsion coatings for inhibition of Listeria on webbed-rind melons: a comparative study with fig and citrus pectins

The objective of this study was to employ pectin-based antimicrobial coatings for inhibition of Listeria on surfaces of whole webbed-rind melons that cause frequent outbreaks of listeriosis. For this purpose, emulsion-based coatings were developed using citrus pectin (CPEC) or pectin extracted from processing wastes of sun-dried figs (FPEC) and eugenol (EUG). The emulsions of FPEC and CPEC with EUG (droplet size range: 1.99–11.22 µm) were highly stable for minimum 10 days at 10 °C. The FPEC-EUG films showed higher flexibility and degree of wettability than CPEC-EUG films. In contrast, CPEC-EUG films had a higher gas barrier performance against oxygen at 50% relative humidity than FPEC-EUG films. The zone inhibition tests showed that FPEC-EUG films are more effective against Listeria innocua than CPEC-EUG films. However, FPEC and CPEC coatings with 2% EUG caused 2.2 and 2.7 decimal inactivation of Listeria on Galia melons within 1 week, respectively. The pectin coatings with EUG could reduce the risk of listeriosis from webbed-rind melons.     

Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films

Lactoperoxidase (LPS), purified directly from bovine rennet whey by Toyopearl-SP cation-exchange chromatography and lyophilized by using dextran as supporting material, maintained almost 70 and 60% of its activity after almost 2 and 5 months storage at −18 °C, respectively. Incorporation of the prepared LPS into alginate films between 0.08 and 0.69 mg/cm² (516–4325 U/cm²) caused the immobilization of most of the enzyme and gave films with LPS activity between 0.05 and 2.8 U/cm², determined in the presence of 8 μM H₂O₂. Between 2 and 24 μM H₂O₂ concentrations, a two-fold increase in H₂O₂ concentration caused 1.5–2.5-fold increase in LPS activity of films incorporated with 0.24–0.28 mg/cm² (1200 U/cm²) LPS. The Q₁₀ and E_a of immobilized enzyme activity between 4 and 16 °C were 1.69 and 34.6 kJ/mol, respectively. However, in the 16–30 °C range, the temperature change had almost no effect on LPS activity of films. The optimal activity of immobilized LPS was observed at pH 6.0, but the enzyme maintained 30–85% of its activity between pH 3.0 and 7.0. The immobilized LPS also had a high stability between pH 4.0 and 6.0. The results of this study showed the good potential of LPS-incorporated alginate films in forming a natural antimicrobial mechanism in different foods.     

Effects of Nisin and Lysozyme on Growth Inhibition and Biofilm Formation Capacity of Staphylococcus aureus Strains Isolated from Raw Milk and Cheese Samples

Effects of nisin and lysozyme on growth inhibition and biofilm formation capacity of 25 Staphylococcus aureus strains isolated from raw milk (13 strains) and cheese (12 strains) were studied. Nisin was tested at concentrations between 0.5 and 25 μg/ml; the growth of all strains was inhibited at 25 μg/ml, but the resistances of strains showed a great variation at lower nisin concentrations. In contrast, lysozyme tested at concentrations up to 5.0 mg/ml showed no inhibition on the growth of strains. Nisin used at the growth inhibitory concentration prevented the biofilm formation of strains, but strains continued biofilm formation at subinhibitory nisin concentrations. Lysozyme did not affect the biofilm formation of 19 of the strains, but it caused a considerable activation in the biofilm formation capacity of six strains. Twelve of the strains contained both biofilm-related protease genes (sspA, sspB, and aur) and active proteases; eight of these strains were nisin resistant. These results suggest a potential risk of S. aureus growth and biofilm formation when lysozyme is used in the biopreservation of dairy products. Nisin can be used to control growth and biofilm formation of foodborne S. aureus, unless resistance against this biopreservative develops.     

Effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea proteins

This study investigated the effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea protein extracts (CPE). The enzyme hydrolysis increased soluble protein content (1.2 to 2-fold) and free radical scavenging activity (1.9 to 3-fold) of hydrolyzed chickpea protein extract (HCPE), but almost unaffected its antioxidant potential in oil-in-water emulsion system and reduced its iron chelating capacity (1.3-fold) and functional properties. The chromatographic fractions of CPE are mainly acidic, while those of HCPE are mainly basic and neutral. The majority of chickpea proteins had pI between 4.5 and 5.5, and molecular weight (MW) between 15 and 40 kDa, while MW of their pepsin hydrolysis products ranged between 6.5 and 14.2 kDa. The main antioxidant proteins in CPE and HCPE fractionated by ultrafiltration had MW greater than 30 kDa and between 2 and 10 kDa, respectively. The chickpea proteins and hydrolysates showed different potentials as functional food ingredients.     

Separation and thermal characterization of ionically and tightly cell-wall-bound pectin methylesterase from cucumbers (Cucumis sativus)

Thermal characteristics of cell-wall-bound pectin methylesterase (PME) from cucumbers were determined. Heat inactivation of PME followed first-order reaction kinetics. Biphasic inactivation curves indicated the presence of heat-labile and heat-stable fractions. Inactivation of PME accelerated above 65??°C. The z values between 70??°C and 80??°C were 7.6??°C and 9.0??°C for heat-stable fractions of ionically (IPME) and tightly cell wall bound PME (TPME), respectively. Temperature optima for the initial activities of IPME and TPME were 65??°C and 60??°C, respectively. However, for longer periods of activity determination, both IPME and TPME showed a temperature optimum at 50??°C. The E _a values for initial activities were 5?kcal mol^–1 (20–65??°C) and 7.2?kcal mol^–1 (20–60??°C) for IPME and TPME, respectively.