Enzymatic synthesis of sugar fatty acid esters in organic solvents is a well-described procedure to synthesize glycolipids. This study aims at replacing these solvents with deep eutectic solvents (DES), a group of solvents that gained more and more interest during the last years, since they can be easily produced from non-toxic resources. Enzymatic glycolipid synthesis in deep eutectic solvents was investigated, employing Candida antarctica lipase B (Novozyme 435) in various deep eutectic solvents. A successful lipase-catalyzed synthesis of glucose fatty acid esters gave proof of this concept, while using the two deep eutectic solvents consisting of choline chloride and urea (CC : U) and choline chloride and glucose (CC : Glc). Additionally the DES consisting of choline chloride and glucose was observed to act as solvent and substrate for the synthesis at the same time.Practical application Glycolipids find applications in many everyday products like cosmetic and pharmaceutical formulations, food and classic cleaning products, utilizing their good detergent or emulsification properties. Glycolipids can, among other routes, be synthesized via lipase-catalyzed reactions, which are often carried out in organic solvents. By replacing these organic solvents with more ecologically friendly solvents like deep eutectic solvents, the reaction might be improved and the amount of waste produced could be reduced.
Surfactants are an essential part of detergent or emulsifier formulations and find applications in food, cleaning, cosmetic and pharmaceutical products. Glycolipids are among the best studied surfactants originating from renewable resources and can be obtained by chemical synthesis, fermentation processes as well as by enzymatic syntheses and have gained considerable interest in recent years. The use of suitable enzymes not only facilitates the synthesis of new tailor‐made glycolipids, but also allows targeted modification of known microbial glycolipids. Thereby, novel glycolipids may arise with enhanced surfactant properties, which might exhibit interesting bioactive properties as well. Here we present an overview of the advantages, strategies and important parameters regarding the enzymatic synthesis and modification of surface‐active glycolipids. Within this article different strategies and advantages of the enzymatic synthesis and modification of glycolipids are discussed.
N-Acetyl-glucosamine fatty acid esters were synthesized by a lipase-catalyzed transesterification with methyl hexanoate and N-acetyl-glucosamine (GlcNAc), which resulted in the formation of 2-(acetylamino)-2-deoxy-6-O-hexanoate-D-glucose, a novel glycolipid. Additionally N-butyryl-glucosamine (GlcNBu) was used for a similar synthesis, leading to the formation of 2-(butyrylamino)-2-deoxy-6-O-hexanoate-D-glucose. The higher hydrophobicity of GlcNBu led to an increase in the overall yield and the initial reaction rate when compared to the reaction with GlcNAc. By pre-dissolving GlcNAc and GlcNBu in dimethyl sulfoxide (DMSO), it was possible to completely dissolve both sugars in the organic solvent, thus further enhancing the initial reaction rate and yield respectively.Practical applications: Glycolipids are used in a wide range of applications, ranging from food, cosmetic, and pharmaceutical formulations, where they can be used as emulsifiers or foaming agents to classic cleaning products, utilizing their good detergent properties. Further applications may include fields like membrane protein extraction, bioremediation, or tertiary oil recovery. Novel glycolipids with tailor-made properties might be useful to improve any of the named applications and widen the diversity of available environmentally friendly surfactants, often termed "green surfactants." Glycolipids are the most prominent example therefrom.
New screening techniques for improved enzyme variants in turbid media are urgently required in many industries such as the detergent and food industry. Here, a new method is presented to measure enzyme activity in different types of substrate suspensions. This method allows a semiquantitative determination of protease activity using native protein substrates. Unlike conventional techniques for measurement of enzyme activity, the BioLector technology enables online monitoring of scattered light intensity and fluorescence signals during the continuous shaking of samples in microtiter plates. The BioLector technique is hereby used to monitor the hydrolysis of an insoluble protein substrate by measuring the decrease of scattered light. The kinetic parameters for the enzyme reaction (V(max,app) and K(m,app)) are determined from the scattered light curves. Moreover, the influence of pH on the protease activity is investigated. The optimal pH value for protease activity was determined to be between pH 8 to 11 and the activities of five subtilisin serine proteases with variations in the amino acid sequence were compared. The presented method enables proteases from genetically modified strains to be easily characterized and compared. Moreover, this method can be applied to other enzyme systems that catalyze various reactions such as cellulose decomposition.
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