Laccase-catalyzed oxidative cross-linking of tyrosine and potato patatin- and lysozyme-derived peptides: Molecular and kinetic study.

Laccase can catalyze the oxidative cross-linking of peptides, which is useful in the production of proteinaceous materials with enhanced functional properties. However, the kinetics and the pathway of this reaction remain unclear. In the present study, laccase-catalyzed oxidative cross-linking reaction was investigated through a combination of computational analysis, kinetic studies and end-product profiling using selected substrate models, including peptide AG-10 (AKKIVSDGNG) (without tyrosine) derived from lysozyme and tyrosine-containing peptide ST-10 (SYMTDYYLST) from potato protein (patatin), and tyrosine.

Lyoprotection and stabilization of laccase extract from Coriolus hirsutus, using selected additives.

The development of stable lyophilized laccase, obtained from Coriolus hirsutus, using a wide range of temperature treatments and storage conditions, was investigated. Using selected lyoprotectants, including, dextran 6 kDa, sucrose and a mixture of sodium benzoate, potassium sorbate and sorbitol (BKSS) (1.5:1.

Microencapsulation of esterified krill oil, using complex coacervation.

The microencapsulation of the esterified krill oil (EKO), obtained from the transesterification of krill oil (KO) with 3,4-dihydroxyphenylacetic acid (DHPA), via complex coacervation and was investigated. The experimental findings showed that the DHPA and phenolic lipids (PLs) in the EKO affected the stability of the gelatine (GE)-EKO emulsion. To improve its stability, the effects of varying the pH of GE and the use of two emulsification devices, including the homogeniser and ultrasonic liquid processor were investigated, where the ultrasonic liquid processor was found to be a relatively more appropriate emulsification device.

Selected dehydrogenases in Yarrowia lipolytica JMY 861: their role in the synthesis of flavor compounds.

The presence of selected dehydrogenases, including alcohol dehydrogenase (ADH-YL) and aldehyde dehydrogenase (ALDH-YL), in Yarrowia lipolytica JMY 861, and their potential role in flavor synthesis were investigated. The experimental findings showed that using reduced form of nicotinamide adenine dinucleotide (NADH) as cofactor, the ADH-YL activity in vitro was 6-fold higher than that with reduced form of nicotinamide adenine dinucleotide phosphate (NADPH); however, under the experimental conditions used in this study, an ALDH-YL activity was not detected. The in situ hexanal reduction reaction was found to be instantaneous; however, when the yeast cells suspension was diluted 150 times, the initial relative hexanal concentration was increased by 84.

Optimization of the Hydrolysis of Safflower Oil for the Production of Linoleic Acid, Used as Flavor Precursor.

Commercial lipases, from porcine pancreas (PPL), Candida rugosa (CRL), and Thermomyces lanuginosus (Lipozyme TL IM), were investigated in terms of their efficiency for the hydrolysis of safflower oil (SO) for the liberation of free linoleic acid (LA), used as a flavor precursor. Although PPL, under the optimized conditions, showed a high degree of hydrolysis (91.6%), its low tolerance towards higher substrate concentrations could limit its use for SO hydrolysis.

Microencapsulation of krill oil using complex coacervation.

The research work was aimed at the development of a process to yield gelatin-gum Arabic multinuclear microcapsules of krill oil (KO), via complex coacervation. On the basis of the experimental results of the screening trials, a three-level-by-three-factor Box-Behnken design was used to evaluate the effects of the ratio of the core material to the wall (RCW; x1), the stirring speed (SP; x2) and the pH (x3) on the encapsulation efficiency (EE). The experimental findings indicated that x3 has the most significant linear and quadratic effects on the EE of KO and a bilinear effect with x1, whereas x2 did not have any significant effect.

Assessment of the antioxidant capacity and oxidative stability of esterified phenolic lipids in selected edible oils.

The research work was aimed at the determination of the antioxidant capacity (AOC) and the oxidative stability of phenolic lipids (PLs), obtained by lipase-catalyzed transesterification of phenolic acids (PAs) with selected edible oils (EOs), including flaxseed (FSO), fish liver (FO), and krill (KO) oils. The statistical analyses (Tukey's test at P < 0.05) revealed that the difference in AOC between that of the esterified FSO (EFSO) and the esterified krill oil (EKO) containing PLs and their control trials of EOs was significant (P < 0.

Lipase-catalyzed synthesis of structured phenolic lipids in solvent-free system using flaxseed oil and selected phenolic acids as substrates.

Structured phenolic lipids (PLs) were obtained by lipase-catalyzed transesterification of flaxseed oil, in a solvent-free system (SFS), with selected phenolic acids, including hydroxylated and/or methoxylated derivatives of cinnamic, phenyl acetic and benzoic acids. A bioconversion yield of 65% was obtained for the transesterification of flaxseed oil with 3,4-dihydroxyphenyl acetic acid (DHPA). However, the effect of the chemical structure of phenolic acids on the transesterification of flaxseed oil in SFS was of less magnitude as compared to that in organic solvent system (OSS).

Properties of selected hemicellulases of a multi-enzymatic system from Penicillium funiculosum.

A multi-enzymatic system from Penicillium funiculosum displayed alpha-L-arabinofuranosidase, endo-1,4-beta-D-xylanase, beta-D-xylosidase and endo-1,3-1,4-beta-D-glucanase activities at high levels over a wide acidic pH range of 2.0 to 5.5.

Activation and stabilization of the hydroperoxide lyase enzymatic extract from mint leaves (Mentha spicata) using selected chemical additives.

The effects of selected lyoprotecting excipients and chemical additives on the specific activity and the thermal stability of the hydroperoxide lyase (HPL) enzymatic extract from mint leaves were investigated. The addition of KCl (5%, w/w) and dextran (2.5%, w/w) to the enzymatic extract, prior to lyophilization, increased the HPL specific activity by 2.

Characterization of selected cellulolytic activities of multi-enzymatic complex system from Penicillium funiculosum.

The presence of endo-1,4-beta-D-glucanase, cellobiohydrolase, and beta-glucosidase activities in a multi-enzymatic complex system from Penicillium funiculosum was investigated. The interesting feature of these enzymes is their synergistic action for the hydrolysis of the native cellulose into glucose units. Both endo-1,4-beta-D-glucanase and cellobiohydrolase showed broader pH activity profiles, with pH optima of 4.

Optimization of chlorophyllase-catalyzed hydrolysis of chlorophyll in monophasic organic solvent media.

The effects of selected reaction parameters, including solvent hydrophobicity, initial water activity, agitation speed, temperature and enzyme concentration, on the biocatalytic efficiency of a chlorophyllase enzymatic extract from Phaeodactylum tricornutum in neat organic solvent media were investigated. The highest chlorophyllase specific activity of 322 nmol hydrolyzed chlorophyll per gram of protein per minute and bioconversion yield of 91% were obtained in the reaction mixture of hexane/2-octanone (98.3:1.

Lipase-catalyzed transesterification of dihydrocaffeic acid with flaxseed oil for the synthesis of phenolic lipids.

Lipase-catalyzed transesterification reaction of dihydrocaffeic acid (DHCA) with flaxseed oil in organic solvent media was investigated. Using equal molar concentration of DHCA and flaxseed oil, only phenolic monoacylglycerols were obtained with a transesterification yield (TY) of 18.9%.

Characterization of sol-gel entrapped chlorophyllase.

Immobilization of membrane proteins remains a challenge compared to soluble proteins. The membrane protein-chlorophyllase was successful entrapped in tetramethoxysilane (TMOS)-based sol-gel in the presence of lipid. Activity was examined against mixing rate, incubation temperature, time, substrate, acetone, and canola oil concentration.

Fourier transform infrared study of lipoxygenase conformation in organic solvent media.

The secondary structure of commercially purified soybean lipoxygenase (EC 1.13.11.

Stability of immobilized soybean lipoxygenase in selected organic solvent media.

The immobilization and biocatalysis of commercially purified soybean lipoxygenase (LOX) type I-B (EC 1.13.11.

Lipase-catalyzed esterification of selected phenolic acids with linolenyl alcohols in organic solvent media.

Lipase-catalyzed esterification of selected phenolic acids with linolenyl alcohols was investigated in selected organic solvent media. The enzyme activity for the esterification of dihydrocaffeic acid with linolenyl alcohol in solvent mixtures of hexane/2-butanone of 75:25 (v/v) and 65:35 (v/v) was 0.88 and 0.

Immobilization and biocatalysis of chlorophyllase in selected organic solvent systems.

Chlorophyllase extract from Phaeodactylum tricornutum was immobilized by physical adsorption on DEAE-cellulose and silica gel as well as by covalent binding on Eupergit C, Eupergit C250L, Eupergit C/ethylenediamine (EDA) and Eupergit C250L/EDA. Although the highest immobilization yield (83-93%) and efficiency (51-53%) were obtained when chlorophyllase extract was immobilized on DEAE-cellulose and silica gel, there was no improvement in the thermal stability of chlorophyllase as compared to that of the free one. The immobilization of chlorophyllase extract on Eupergit C250L/EDA resulted by a high recovery of enzymatic activity, with an immobilization efficiency of 44%, and promoted a higher stabilization of chlorophyllase (four times) in the aqueous/miscible organic solvent medium.

Lipase-catalyzed biosynthesis of cinnamoylated lipids in a selected organic solvent medium.

Biosynthesis of cinnamoylated lipids through the lipase-catalyzed transesterification reaction of cinnamic acid with triolein was investigated in organic solvent media. Electrospray ionization-mass spectroscopy (ESI-MS) structural analysis of the reaction mixture revealed the formation of two major end products, monoleyl-1(3)-cinnamate and dioleyl-2-cinnamate. Decreasing the molar ratio of cinnamic acid to triolein from 1:1 to 1:4.

Characterization of tyrosinase- and polyphenol esterase-catalyzed end products using selected phenolic substrates.

The oxidative end products that result from the biocatalysis of tyrosinase (PPO) and/or a polyphenol esterase (PPE) extract have been investigated simultaneously in model systems containing selected phenolic compounds as substrates. The spectrophotometric scanning of brown color, formed in the presence of both PPO and PPE, showed a decrease in the absorbance compared to that obtained with PPO only. Graphical analyses of the iterative spectra of oxidized phenolic end products by PPO confirmed the presence of, at least, three kinetically related absorbing species.

Encapsulation in the food industry: a review.

Encapsulation involves the incorporation of food ingredients, enzymes, cells or other materials in small capsules. Applications for this technique have increased in the food industry since the encapsulated materials can be protected from moisture, heat or other extreme conditions, thus enhancing their stability and maintaining viability. Encapsulation in foods is also utilized to mask odours or tastes.

Biocatalysis of immobilized chlorophyllase in a ternary micellar system.

The immobilization of chlorophyllase was optimized by physical adsorption on various inorganic supports, including alumina, celite, Dowex-1-chloride, glass beads and silica gel. The enzyme was also immobilized in different media, including water, Tris-HCl buffer solution and a ternary micellar system containing Tris-HCl buffer solution, hexane and surfactant. The highest immobilization efficiency (84.

Characterization of an endo-1,3-beta-D-glucanase produced during the interaction between the mycoparasite Stachybotrys elegans and its host Rhizoctonia solani.

The mycoparasite Stachybotrys elegans produces, in addition to a previously purified 94-kDa 1,3-beta-glucanase, at least three extracellular 1,3-beta-glucanases (75, 110, and 180 kDa) when grown on purified cell wall of Rhizoctonia solani. We purified to homogeneity an endo-1,3-beta-glucanase of 75 kDa which possesses a low K(m) value of 20 micrograms laminarin.mL-1 and is most active at pH 5.

Characterization of hydroperoxides and carbonyl compounds obtained by lipoxygenase extracts of selected microorganisms.

Partially purified lipoxygenase (LOX) extracts were obtained from Fusarium proliferatum, Fusarium oxysporum, Chlorella pyrenoidosa, and Saccharomyces cerevisiae; the enzymatic extract of F. proliferatum showed the highest LOX activity while those of F. oxysporum and S.