Abstract: Disclosed is a process for the preparation of an interfacial enzyme immobilized on an insoluble support, by providing a bi-phase system comprised of an aqueous buffer solution and at least one first organic solvent; mixing said interfacial enzyme with the bi-phase system provided; adding the support to the obtained mixture and mixing; and isolating from the mixture obtained in the last step the interfacial enzyme immobilized on said support. The produced enzyme is locked in its catalytically active confirmation, and thus exhibits improved activity and stability. Also disclosed are uses of the produced enzymes, particularly in the preparation of biodiesel.

Abstract: Disclosed are an enzymatic batchwise or continuous process for the production of fatty acid alkyl esters for use in the biofuels, food and detergent industries and a system therefor. The process utilizes enzymes immobilized on a hydrophobic resin mixed with a fatty acid source and an alcohol or alcohol donor in the presence of an alkaline or mild alkaline aqueous buffer, or in the presence of water or aqueous solution. The production process for fatty acid alkyl esters is carried out by transesterification or esterification simultaneously or sequentially. The biocatalyst activity is maintained with no significant activity losses in multiple uses and also avoids the accumulation of glycerol and water by-products or other hydrophilic compounds on the biocatalyst.

Abstract: Disclosed is an enzymatic process for the preparation of fatty acid alkyl esters, particularly fatty acids methyl esters (biodiesel) in a solvent-free microaqueous system, from a fatty acid source and an alcohol or alcohol donor, employing a robust lipase preparation that comprises at least two lipases separately or jointly immobilized on a suitable support, where one of the lipases has increased affinity to partial glycerides, another is sn-1,3 positional specific, and an optional third lipase has high selectivity towards sn-2 position of the glycerol backbone of the fatty acid source.

Abstract: A process for the preparation of short-chain alkyl esters of fatty acids, preferably fatty acid methyl esters (biodiesel) in solvent-free system is disclosed. In particular, the process comprises (a) providing a fatty acid source, (b) stepwise adding a short-chain free alcohol, preferably methanol, or any other alcohol donor, to said fatty acid source in the presence of a lipase preparation and (c) allowing the reaction to proceed under suitable conditions, until said fatty acid source triglycerides are converted to fatty acid methyl esters (FAME). The lipase preparation comprises at least two lipases. The two lipases being separately or jointly immobilized on a suitable support and wherein at least one of the lipases has increased affinity for partial glycerides and at least one of the lipases is sn-1,3 positional specific.

Abstract: Disclosed are preparations of modified interfacial enzymes, particularly lipases and phospholipases, immobilized on a solid support, wherein the enzyme is surrounded by hydrophobic microenvironment, thereby protected from deactivation and/or aggregation in the presence of hydrophilic agents, substrates and/or reaction products. The enzyme may be protected by being covalently bonded with lipid groups which coat the enzyme, or by being immobilized or embedded in a hydrophobic solid support. Also disclosed are processes for the preparation of the hydrophobically protected enzymes. The enzymes may be efficiently used in the preparation of biodiesel.

Abstract: Heavy metal-containing nano-liposome particles and their use in treating, for example, immune-related disorders, such as, cancer and inflammatory conditions, and metal deficiency-related diseases are described. The particles also can be used in diagnostic methods. The particles can contain gold, platinum or iron.

Abstract: Disclosed is a process for the preparation of an interfacial enzyme immobilized on an insoluble support, by providing a bi-phase system comprised of an aqueous buffer solution and at least one first organic solvent; mixing said interfacial enzyme with the bi-phase system provided; adding the support to the obtained mixture and mixing; and isolating from the mixture obtained in the last step the interfacial enzyme immobilized on said support. The produced enzyme is locked in its catalytically active confirmation, and thus exhibits improved activity and stability. Also disclosed are uses of the produced enzymes, particularly in the preparation of biodiesel.

Abstract: A process for the preparation of short-chain alkyl esters of fatty acids, preferably fatty acid methyl esters (biodiesel) in solvent-free system is disclosed. In particular, the process comprises (a) providing a fatty acid source, (b) stepwise adding a short-chain free alcohol, preferably methanol, or any other alcohol donor, to said fatty acid source in the presence of a lipase preparation and (c) allowing the reaction to proceed under suitable conditions, until said fatty acid source triglycerides are converted to fatty acid methyl esters (FAME). The lipase preparation comprises at least two lipases. The two lipases being separately or jointly immobilized on a suitable support and wherein at least one of the lipases has increased affinity for partial glycerides and at least one of the lipases is sn-1,3 positional specific.

Abstract: A new enzymatic process for preparing 1,2-diacylated phospholipids using an enzyme preparation possessing phospholipase activity towards acylation at the sn-1 and sn-2 sites in a microaqueous reaction system. More particularly, the 1,2-diacyl-phospholipids produced according to the esterification/transesterification process are obtainable in high yield and purity and carry identical desired carboxylic acid, preferably fatty acid, acyl groups at the sn-1 and sn-2 positions. The process involves esterification/transesterification (acylation) of a glycerophospholipid, preferably glycerophosphoryl choline (GPC) with a desired carboxylic acid, preferably fatty acid, or their derivatives in the presence of the above mentioned appropriate enzyme preparation.

Abstract: A composition of at least one diacylglycerol and at least one phytosterol and/or phytostanol ester dissolved or dispersed in an edible oil and/or edible fat, and further optionally containing monoglycerides. Phytosterol esters may be beta-sitosterol, campesterol, stigmasterol and brassicasterol esters. Phytostanol esters may be stigmasterol, campestanol and sitostanol. The phytosterol and/or phytostanol esters are preferably esters of C14-C22, preferably C16-C18 saturated or unsaturated fatty acids, particularly oleic, linoleic, linolenic, palmitic and stearic acids. The diacylglycerol(s) are preferably 1,3-di-fatty acyl glycerol(s). A process for preparing compositions enriched with triacylglycerol(s) and phytosterol and/or phytostanol esters of mainly unsaturated fatty acid(s) or of mainly saturated fatty acid(s). Dietary food supplements and alimentary products derived from the above compositions.

Abstract: A new enzymatic process for preparing 1,2-diacylated phospholipids using an enzyme preparation possessing phospholipase activity towards acylation at the sn-1 and sn-2 sites in a microaqueous reaction system. More particularly, the 1,2-diacyl-phospholipids produced according to the esterification/transesterification process are obtainable in high yield and purity and carry identical desired carboxylic acid, preferably fatty acid, acyl groups at the sn-1 and sn-2 positions. The process involves esterification/transesterification (acylation) of a glycerophospholipid, preferably glycerophosphoryl choline (GPC) with a desired carboxylic acid, preferably fatty acid, or their derivatives in the presence of the above mentioned appropriate enzyme preparation.

Abstract: The invention relates to a process for the selective alcoholysis of a free sterol, by contacting said free sterol with a fat-based product, optionally with the addition of carboxylic fatty acid(s) and/or ester derivative(s) thereof that are not derived from said fat-based product, in the presence of an immobilized lipase complex which may optionally be surfactant-coated, which complex possesses a high level of sterol-specific alcoholytic and/or esterfication activity and minimal acidolytic and transesterification activities. The fat-based product is a nutritional product or food, particularly butterfat, or a cosmetic or cosmetic or cosmetic-related product. The process may be used for preparing substantially cholesterol-free fat-based products, particularly products containing butterfat, by selectively esterfying any free cholesterol contained therein by the immobilized, preferably surfactant coated lipase.

Abstract: A catalyst preparation comprising an insoluble matrix and an enzyme complex immobilized onto said insoluble matrix, characterized in that the matrix contains active carbon. The content of the active carbon is preferably in an amount of 0.1 to 70% by weight, more preferably 1 to 40% by weight and most preferably 3 to 20% by weight, relative to the entire matrix. The enzyme, particularly a lipase, is preferably coated with a surfactant. The inorganic insoluble matrix is preferably a silica-based matrix or an ion-exchange resin. The catalyst preparation of the invention is intended for use as a catalyst in esterification, inter-esterification and trans-esterification reactions.

Abstract: A lipase preparation is prepared containing a surfactant-coated lipase complex immobilized onto an insoluble matrix. A preferred surfactant is a fatty acid polyol ester such as sorbitan monostearate (SMS). The lipase preparation may be provided in granulated form or in an organic solvent, and can be used in esterifying, inter-esterifying, trans-esterifying and alcoholysing reactions with no added water. The lipase preferably has 1,3-positional specificity with respect to triacylglycerols, and the insoluble matrix may be modified with a fatty acid derivative. A lipase in aqueous medium is contacted with a surfactant to coat the lipase with the surfactant, and the coated lipase is immobilized onto an insoluble matrix to produce the lipase preparation which may be dried such as by freeze drying. Alternatively, the lipase may be first contacted with the insoluble matrix, and thereafter with the surfactant.