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At least 19 recordsLinked to original sources
PubMed1990

Immobilization of biocatalysts with poly(vinyl alcohol) supports.

Two polymer materials, poly(vinyl alcohol) (PVA) superfine fibers and photocrosslinkable PVA bearing styrylpyridinium groups, have been developed to immobilize biocatalysts. The former has a large surface consisting of relatively large-size pores and the fibers can immobilize a large amount of biocatalyst on their surface by ionic interaction. The latter entraps many kinds of biocatalysts by cyclodimerization caused by visible light irradiation. The biocatalysts on/in these supports maintain high activity and thermal stability. These materials can easily be formed into various shapes suitable for various applications. A new bioreactor system was constructed for evaluating a variety of biocatalysts and supports.

Cross-Linking Reagents↗
PubMed1990

Determination of oxygen profiles in biocatalyst particles by means of a combined polarographic oxygen microsensor.

When studying the effect of immobilization of enzymes or whole cells on the conversion of substrate, more information is gained if measurements of substrate inside the biocatalyst particles are possible. With the methods used until now, only measurements outside the particle can be performed. In this article a method for measuring oxygen profiles in a biocatalyst particle under steady state conditions is described. The biocatalyst particle was made of agarose and contained the enzyme L-lactate 2-monooxygenase. This enzyme decarboxylates lactic acid to acetic acid in the presence of oxygen. The experiments were carried out in a flow chamber with the use of a micromanipulator and a stereomicroscope. The data were sampled by means of a computer. Four different profiles were measured using four different enzyme concentrations. The measured oxygen profiles were reproducible and the signal was very stable. It was also possible to measure the boundary layer around the particle. With the use of the oxygen microsensor, measurements in a biocatalyst particle could be performed accurately, giving way for model validation.

Biosensing Techniques↗
PubMedDate not supplied

[Stability of biocatalysts on the basis of carrageenan-immobilized Escherichia coli during continuous synthesis of L-malic acid].

Continuous enzymatic synthesis of L-malic acid from potassium fumarate in packed-bed flow reactors was investigated. Carrageenan-immobilized Escherichia coli cells were used as a biocatalyst. The operational stability of the biocatalyst fumarase activity was studied, and conditions for preserving high activity of the biocatalyst were determined.

Bacteriological Techniques↗
PubMed1992

Characterization and use of a penicillin acylase biocatalyst.

A complete characterization of a penicillin acylase biocatalyst is presented, including the determination of physicochemical and kinetic parameters. Stability studies are detailed in terms of both storage temperature and pH as well as operational stability after 150 batch reactions of two hours duration each. An Arrhenius-type model was used to simulate the effect of pH on biocatalyst stability. A kinetic model is proposed to describe batch and continuous stirred tank reactors and to predict the long-term behavior of the process.

Biotechnology↗
PubMed1991

Determination of biocatalyst consumption in an aminopeptidase process using automated sample preparation and high-performance liquid chromatography.

A rapid and sensitive method has been developed for the determination of the biocatalyst consumption in the chemo-enzymic production of optically pure natural and synthetic alpha-H-amino acids. It is based on automated sample preparation from an enzymic reaction mixture, reversed-phase high-performance liquid chromatographic separation, post-column reaction and fluorimetric detection. The assay procedure has been applied to the enzymic conversion of racemic norvaline amide into L-norvaline, catalysed by an L-specific aminopeptidase from Pseudomonas putida. Both norvaline amide and norvaline can be analysed in a single assay in the low nanogram range. The method yields reproducible results and requires 30 min from the time of sampling the enzymic reaction mixture to quantitation. The reaction mixture is automatically sampled and analysed several times during the course of the reaction. With the results obtained a conversion curve can be constructed from which the exact biocatalyst consumption can be calculated. By adaptation of the mobile phase, the method can also be applied to other amino acid amides used as substrates in the aminopeptidase reaction.

Aminopeptidases↗
PubMed1989

[Ways of developing the first and second generation biocatalysts for antibiotic production].

Methods for development of bioengineering systems of different types useful in synthesis and transformation of antibiotics are discussed. It was shown that in development of monoenzymatic biocatalysts on the basis of immobilized cells and in preparation of immobilized cultures producing secondary metabolites with enzymological engineering directed action on the cells could be provided which made it possible to establish highly efficient bioengineering systems. Various means for providing the directed action and method for estimation of the carrier-culture interation are proposed. The prospects of using the second generation biocatalysts in improvement of the processes for production of antibiotics are described.

Catalysis↗
PubMed2026

Marine Vibrio Biocatalysts as Unique Green Transformation (GX) Tools at the Time to Sustainable Development Goals (SDGs).

Vibrios have sustained various types of ocean ecosystems, being key players in marine mineral cycles and essential partners in specific groups of marine life. Observed genome plasticity and metabolic versatility are some of the unique biological features of vibrios, and these traits could contribute in expanding their ecological niche in marine environments. Vibrios are now recognized as ecophysiologically essential microbial species for our planet. At the time to "Sustainable Development Goals" (SDGs), their genome plasticity and metabolic versatility have also been studied with the aim of solving global issues such as energy production and plastic pollution by creating new microbial biocatalysts. Here, we introduce recent progress on the application of vibrios aiming towards green transformation (GX).

Vibrio↗
PubMed1992

Silicone-immobilized biocatalysts effective for bioconversions in nonaqueous media.

A hydrophobic silicone polymer could be effectively applied to immobilization of two kinds of biocatalysts operating in organic media. Horse liver alcohol dehydrogenase, which was solubilized in a small amount of water, or deposited on water-filled hydrophilic particles, was immobilized in this material. This configuration of the preparation involving finely dispersed aqueous phase permitted a simple packed-bed operation for the enzymatic oxidation of alcohol and reduction of aldehyde with a coupled-substrate NAD(H) recycling in n-hexane. Another example was the immobilization of Nocardia corallina which catalysed epoxidation of liquid alkenes such as 1-tetradecene, 1-octene, and styrene in the presence of n-hexadecane. In order to adjust the hydrophobicity-hydrophilicity balance of the support, it was effective to immobilize the cells in a mixed matrix composed of silicone polymer and Ca-alginate gel. The optimum composition of the mixed matrix, which yielded the highest productivity of epoxide, was 80-90% silicone + 20-10% alginate for the production of 1,2-epoxytetradecane, 40-50% silicone + 60-50% alginate for 1,2-epoxyoctane, and almost 0% silicone + 100% alginate for styrene oxide. This significant change of the optimum composition was primarily associated with the degree of substrate inhibition.

Alcohol Dehydrogenase↗
PubMed1990

Continuous itaconic acid production by immobilized biocatalysts.

The continuous itaconic acid production from sucrose with Aspergillus terreus TKK 200-5-3 mycelium immobilized on polyurethane foam cubes was optimized in column bioreactors using statistical experimental design and empirical modelling. The highest itaconic acid product concentration calculated on the basis of the obtained model was 15.8 g l-1 in the investigated experimental area, when sucrose concentration was 13.5%, aeration rate 150 ml min-1 and residence time 178 h. From sucrose with immobilized A. terreus TKK 200-5-3 mycelium itaconic acid production was stable for at least 4.5 months in continuous column bioreactors. In comparison, using glucose as substrate and immobilized A. terreus TKK 200-5-1 mycelium as biocatalyst similar stability was obtained with higher product concentration. The omission of copper sulphate from the production medium gave the highest itaconic acid product concentration (26 g l-1) from 9% glucose with 0.25% ammonium nitrate and 0.095% magnesium sulphate.

Aspergillus↗
PubMed1992

New applications of biocatalysts.

The development of new biocatalytic applications continues to advance in several directions. Over the past year, new enzymes have been discovered and their potential in biocatalyst applications has been researched. In addition, new chemical and genetic modifications have been made in the development of novel fermentation processes.

Biotechnology↗
PubMed1991

Kinetically controlled synthesis of dipeptides using ficin as biocatalyst.

The application of the sulfhydryl protease ficin as biocatalyst is proposed as a novel method for enzyme-catalyzed synthesis of dipeptides. The negligible peptidase but considerable esterase activity at alkaline pH facilitated the kinetically controlled formation of peptide bonds by coupling the ester substrates Z-Ala-OMe and Z-Gly-OMe with L-alanine, D-alanine, L-glutamine, D-glutamine and L-Cys(acetamidomethyl) respectively. The reaction is accomplished without the occurrence of secondary peptide hydrolysis. Under optimum reaction conditions (pH 9.2, high ratio nucleophile/carboxyl component, 4.8% ethanol, 40 degrees C), the peptide yields ranged from 5 to 91%, depending on the structure of the amino and/or carboxyl component. No racemization was observed in the enzymatic reaction. Application of short-chain peptides has been advocated recently in clinical nutrition. Ficin-catalyzed peptide synthesis might be an attractive biotechnological approach for the synthesis of suitable dipeptides in this respect.

Amino Acids↗
PubMed2026

Unlocking the molecular engineering of Geobacillus glycoside hydrolases as a source of industrial biocatalysts.

This review examines Geobacillus sensu stricto as a source of thermostable glycoside hydrolases (GH) for biomass conversion, food processing, and enzyme engineering. Recent peer-reviewed literature was assessed with emphasis on taxonomy, genome-based Carbohydrate-Active Enzymes (CAZyme) prediction, biochemical validation, structural data, and engineering case studies. Taxonomic boundaries were interpreted using current Anoxybacillaceae frameworks, with Parageobacillus treated as a related comparator rather than as Geobacillus. The strongest evidence supports GH13 alpha-amylases, xylan-active systems, beta-xylosidases, and selected accessory enzymes. Recent studies also show that genome mining must be coupled with enzymatic assays and product profiling because CAZyme annotation alone does not prove industrial function. Molecular engineering has improved relevant traits, including the longer thermal half-life of engineered G. stearothermophilus alpha-amylase variants, the increased catalytic efficiency of oligo-alpha-1,6-glucosidase variants, and improved AmyS expression in Bacillus subtilis. Geobacillus glycoside hydrolases are best interpreted as process-specific, engineerable biocatalytic templates. Their translation requires reliable taxonomy, functional validation, structural interpretation, scalable expression and testing on realistic substrates. This synthesis also recognises current limitations: many predicted CAZymes still lack biochemical validation, complete cellulolytic systems remain less mature than xylan- and starch-active systems, and scale-up data remain scarce.

Geobacillus↗