skin permeation of flavonoid esters enzymatically derived from natural oils: release mechanism from gel emulsion, stability, and dermatological compatibility.

Due to their broad spectrum of biological activities and attractive pharmacological properties, flavonoids are very promising molecules for application in skin care products. In this study, phloridzin and naringin medium- and long-chain fatty acid esters were enzymatically synthesized in reaction with natural oils (coconut and linseed oil) and transdermal delivery of synthesized esters through artificial Strat-M membrane was investigated. Experimental results were succesfully fitted using Peppas and Sahlin model which includes the phase.

Valorisation of Blackcurrant Pomace by Extraction of Pectin-Rich Fractions: Structural Characterization and Evaluation as Multifunctional Cosmetic Ingredient.

Blackcurrant pomace is a widely available waste stream derived from the industrial production of juice rich in pectin and unextracted polyphenols. Since pectin, an emerging class of gastrointestinal prebiotics, is also a common cosmetic ingredient, the aim of this work was to evaluate blackcurrant pomace as a source of pectin-rich fractions suitable for application in prebiotic cosmetics. Hereby, this raw material was valorised by sequential extraction of acid-soluble (by citric acid, CAP) and Ca-bound (by ammonium oxalate, AOPP) pectic polysaccharides.

Assessment of Enzymatically Derived Blackcurrant Extract as Cosmetic Ingredient-Antioxidant Properties Determination and In Vitro Diffusion Study.

Blackcurrant is an anthocyanin-rich berry with proven antioxidant and photoprotective activity and emerging prebiotic potential, widely applied in cosmetic products. Hereby, highly efficient enzyme-assisted extraction of blackcurrant polyphenols was performed, giving extract with very high antioxidant activity. Obtained extract was characterized in terms of anthocyanin composition, incorporated into three different cosmetic formulations and subjected to Franz cell diffusion study.

In vitro assessment of skin permeation properties of enzymatically derived oil-based fatty acid esters of vitamin C.

Current topical formulations containing vitamin C face limitations in therapeutic effectiveness due to the skin's selective properties that impede drug deposition. Consequently, the widespread use of toxic and irritating chemical permeation enhancers is common. Hereby, we investigated enzymatically derived fatty acid ascorbyl esters (FAAEs) obtained using natural oils for their skin permeation properties using the Strat-M® skin model in a Franz cell diffusion study.

Sunflower Meal Valorization through Enzyme-Aided Fractionation and the Production of Emerging Prebiotics.

Recently, there has been a burgeoning interest in harnessing the potential of biomass and industry byproducts for the development of novel products and materials. In particular, this study explored the efficient valorization of sunflower meal (SFM), an underutilized byproduct of the oil extraction industry, usually discarded or used as low-value animal feed through enzyme-aided fractionation, specifically targeting the extraction and conversion of its abundant carbohydrate component, xylan, into emerging prebiotic compounds-xylo-oligosaccharides (XOSs)-which are recognized as promotors of a healthy gut microbiome and overall human wellbeing. An enzymatic treatment using Alcalase 2.

Artificial Manganese Metalloenzymes with Laccase-like Activity: Design, Synthesis, and Characterization.

Laccase is an oxidase of great industrial interest due to its ability to catalyze oxidation processes of phenols and persistent organic pollutants. However, it is susceptible to denaturation at high temperatures, sensitive to pH, and unstable in the presence of high concentrations of solvents, which is a issue for industrial use. To solve this problem, this work develops the synthesis in an aqueous medium of a new Mn metalloenzyme with laccase oxidase mimetic catalytic activity.

Production of prebiotic enriched maple syrup through enzymatic conversion of sucrose into fructo-oligosaccharides.

Maple syrup, a popular natural sweetener has a high content of sucrose, whose consumption is linked to different health issues such as obesity and diabetes. Hence, within this paper, the conversion of sucrose to prebiotics (fructo-oligosaccharides, FOS) was proposed as a promising approach to obtaining a healthier, value-added product. Enzymatic conversion was optimized with respect to key experimental factors, and thereafter derived immobilized preparation of fructosyltransferase (FTase) from Pectinex® Ultra SP-L (FTase-epoxy Purolite, 255 IU/g support) was successfully utilized to produce novel functional product in ten consecutive reaction cycles.

Prebiotic effect of galacto-oligosaccharides on the skin microbiota and determination of their diffusion properties.

Objective: Recently, prebiotics are attracting plenty of attention in the field of skin care, since it is found that they are able to support the balance of beneficial and harmful microorganisms on the skin, and accordingly prevent several skin conditions associated with microbial imbalance. Topical application of prebiotics, although insufficiently investigated, holds great promise in improving skin health. The purpose of this research was to determine the prebiotic potential of galacto-oligosaccharides (GOS) for skin microbiota and suitability for incorporation in different topical formulations, and finally, provide insights into their diffusion properties.

Amino-modified kraft lignin microspheres as a support for enzyme immobilization.

In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing β-galactosidase from and laccase from expressed in (Novozym® 51003) onto A-LMS. Two types of A-LMS were investigated, with different emulsifier concentrations (5 wt% and 10 wt%), and microspheres produced using 5 wt% of emulsifier (A-LMS_5) showed adequate pore shape, size and distribution for enzyme attachment. The type of interactions formed between enzymes (β-galactosidase and laccase) and A-LMS_5 microspheres demonstrated that β-galactosidase is predominantly attached electrostatic interactions while attachment of laccase is equally governed by electrostatic and hydrophobic interactions.

Response Surface Methodology As a New Approach for Finding Optimal MALDI Matrix Spraying Parameters for Mass Spectrometry Imaging.

Automated spraying devices have become ubiquitous in laboratories employing matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI), in part because they permit control of a number of matrix application parameters that can easily be reproduced for intra- and interlaboratory studies. Determining the optimal parameters for MALDI matrix application, such as temperature, flow rate, spraying velocity, number of spraying cycles, and solvent composition for matrix application, is critical for obtaining high-quality MALDI-MSI data. However, there are no established approaches for optimizing these multiple parameters simultaneously.

Evaluation of β-galactosidase from Lactobacillus acidophilus as biocatalyst for galacto-oligosaccharides synthesis: Product structural characterization and enzyme immobilization.

β-Galactosidase is an important industrial enzyme that catalyzes reaction of lactose hydrolysis and recently more interesting reaction of transgalactosylation, yielding a highly valuable group of prebiotic compounds named galacto-oligosaccharides (GOS). In this paper, parameters for achieving high yields of tailor-made GOS using crude β-galactosidase obtained from Lactobacillus acidophilus ATCC 4356, probiotic bacteria regarded as safe for human consumption, were optimized. At the same time, detailed structural elucidation of obtained GOS was conducted, and it was concluded that β-galactosidase from L.

Immobilization of dextransucrase on functionalized TiO supports.

The TiO based hybrid supports with different functional groups (amino, glutaraldehyde or epoxy) were prepared and their influence on immobilization of dextransucrase (DS) was studied. Novel synthetic route for surface modification of TiO with amino and glutaraldehyde groups was developed taking advantage of charge transfer complex (CTC) formation between surface Ti atoms and salicylate-type of ligand (5‑aminosalicylic acid (5-ASA)). The proposed coordination of 5-ASA to the surface of TiO powder and optical properties of CTC was presented.

Covalent Immobilization of Enzymes on Eupergit Supports: Effect of the Immobilization Protocol.

A selection of best combination of adequate immobilization support and efficient immobilization method is still a key requirement for successful application of immobilized enzymes on an industrial level. Eupergit supports exhibit good mechanical and chemical properties and allow establishment of satisfactory hydrodynamic regime in enzyme reactors. This is advantageous for their wide application in enzyme immobilization after finding the most favorable immobilization method.

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases.

A commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors. Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85% of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained.

Immobilization of Candida antarctica lipase B onto Purolite MN102 and its application in solvent-free and organic media esterification.

The aim of this study was to develop simple and efficient method for immobilization of Candida antarctica lipase B onto hydrophobic anion exchange resin Purolite MN102 and to apply immobilized catalyst for the enzymatic synthesis of two valuable esters-isoamyl acetate and L-ascorbyl oleate. At optimized conditions (1 M phosphate buffer pH = 7, 7 h at 25 °C, and 18.75 mg of offered proteins g of support), immobilized lipase with hydrolytic activity of 888.

Structural Elucidation of Enzymatically Synthesized Galacto-oligosaccharides Using Ion-Mobility Spectrometry-Tandem Mass Spectrometry.

Galacto-oligosaccharides (GOS) represent a diverse group of well-characterized prebiotic ingredients derived from lactose in a reaction catalyzed with β-galactosidases. Enzymatic transgalactosylation results in a mixture of compounds of various degrees of polymerization and types of linkages. Because structure plays an important role in terms of prebiotic activity, it is of crucial importance to provide an insight into the mechanism of transgalactosylation reaction and occurrence of different types of β-linkages during GOS synthesis.

Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry.

Background: Biocatalysts are a promising alternative for the production of natural flavor compounds. Candida rugosa lipase (CRL) is a particularly important biocatalyst owing to its remarkable efficiency in both hydrolysis and synthesis. However, additional stabilization is necessary for successful industrial implementation.

Influence of fatty acid on lipase-catalyzed synthesis of ascorbyl esters and their free radical scavenging capacity.

Fatty acid (FA) ascorbyl esters are recently emerging food, cosmetic, and pharmaceutical additives, which can be prepared in an eco-friendly way by using lipases as catalysts. Because they are amphiphilic molecules, which possess high free radical scavenging capacity, they can be applied as liposoluble antioxidants as well as emulsifiers and biosurfactants. In this study, the influence of a wide range of acyl donors on ester yield in lipase-catalyzed synthesis and ester antioxidant activity was examined.

The specificity of α-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylation.

Our investigation of the catalytic properties of Saccharomyces cerevisiae α-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e.

Dual effect of benzyl alcohol on α-glucosidase activity: efficient substrate for high yield transglucosylation and non-competitive inhibitor of its hydrolytic activity.

Benzyl alcohol, a potent anesthetic and bacteriostatic, can be efficiently glucosylated by α-glucosidase from Saccharomyces cerevisiae to produce benzyl alcohol α-glucoside with a 75% yield. However, while studying the transglucosylation reaction conditions, it was found out that benzyl alcohol is a non-competitive inhibitor of α-glucosidase's hydrolytic activity (Ki=18mM, toward maltose). Due to its interesting ability to be glycosylated by the enzyme and to inhibit its hydrolytic activity, we proposed a plausible mechanism for the phenolic α-glucosydase inhibitor's binding, since the mechanism of inhibition has not yet been elucidated.

Lipase-catalyzed synthesis of ascorbyl oleate in acetone: optimization of reaction conditions and lipase reusability.

Lipase-catalyzed ascorbyl oleate synthesis is eco-friendly and selective way of production of liposoluble biocompatible antioxidants, but still not present on an industrial level due to the high biocatalyst costs. In this study, response surface methodology was applied in order to estimate influence of individual experimental factors, identify interactions among them, and to determine optimum conditions for enzymatic synthesis of ascorbyl oleate in acetone, in terms of limiting substrate conversion, product yield, and yield per mass of consumed enzyme. As a biocatalyst, commercial immobilized preparation of lipase B from Candida antarctica, Novozym 435, was used.

Synthesis of aliphatic esters of cinnamic acid as potential lipophilic antioxidants catalyzed by lipase B from Candida antarctica.

Immobilized lipase from Candida antarctica (Novozyme 435) was tested for the synthesis of various phenolic acid esters (ethyl and n-butyl cinnamate, ethyl p-coumarate and n-butyl p-methoxycinnamate). The second-order kinetic model was used to mathematically describe the reaction kinetics and to compare present processes quantitatively. It was found that the model agreed well with the experimental data.

Specificity of maltase to maltose in three different directions of reaction: hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis.

Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor.

Novel glycoside of vanillyl alcohol, 4-hydroxy-3-methoxybenzyl-α-D-glucopyranoside: study of enzymatic synthesis, in vitro digestion and antioxidant activity.

Novel glucoside of physiological active vanillyl alcohol was synthesized for the first time using maltase from Saccharomyces cerevisiae as catalyst, and established its structure as 4-hydroxy-3-methoxybenzyl-α-D: -glucopyranoside. The key reaction factors for this transglucosylation reaction were optimized using response surface methodology and the highest yield so far in maltase catalyzed transglucosylation reaction was obtained. It was found out that optimum temperature of reaction was 37 °C, optimal maltose concentration was 60% (w/v), optimal pH was 6.