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JournalISSN: 1024-2422

Biocatalysis and Biotransformation 

Taylor & Francis
About: Biocatalysis and Biotransformation is an academic journal published by Taylor & Francis. The journal publishes majorly in the area(s): Lipase & Triacylglycerol lipase. It has an ISSN identifier of 1024-2422. Over the lifetime, 1304 publications have been published receiving 20276 citations.


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Journal ArticleDOI
TL;DR: The C. antarctica B-lipase is an example of an enzyme for which its specificity has been predicted based on the crystal structure and modeling of the active site region and a very close correlation is found.
Abstract: The application of the B-component lipase from the yeast Candida antarctica in organic synthesis is reviewed. This enzyme has been found to be a particularly efficient and robust lipase catalyzing a surprising diversity of reactions including many different regio- and enantio-selec-tive syntheses. Furthermore, the C. antarctica B-lipase is an example of an enzyme for which its specificity has been predicted based on the crystal structure and modeling of the active site region. This prediction is compared to experimental observations and a very close correlation is found.

642 citations

Journal ArticleDOI
TL;DR: The most recent developments in the applications of biocatalysts inside inorganic sol-gel matrices, in particular regarding biosensors and chemical synthesis are presented.
Abstract: In the past decade, the encapsulation of enzymes inside inorganic sol-gel matrices has become a generic method to prepare efficient biocatalysts which are easy to recycle. In this review, the sol-gel processes useful for enzyme encapsulation, (mostly sol-gel silica) are outlined. Then, the most recent developments in the applications of such biocatalysts are presented, in particular regarding biosensors and chemical synthesis. Finally, a special attention is addressed to the types of interactions which are considered to prevail between the enzyme or the substrates and products, and the matrix, in these materials.

349 citations

Journal ArticleDOI
TL;DR: This review describes a novel, versatile and effective methodology for enzyme immobilization, namely, as cross-linked enzyme aggregates (CLEAs), which is applicable to a wide variety of enzymes, including cofactor-dependent oxidoreductases and lyases, and amenable to rapid optimization.
Abstract: The key to obtaining optimum performance of an enzyme is often a question of devising an effective method for its immobilization. This review describes a novel, versatile and effective methodology for enzyme immobilization, namely, as cross-linked enzyme aggregates (CLEAs). The method is exquisitely simple – involving precipitation of the enzyme from aqueous buffer followed by cross-linking of the resulting physical aggregates of enzyme molecules – and amenable to rapid optimization. It is applicable to a wide variety of enzymes, including cofactor-dependent oxidoreductases and lyases, and affords stable, recyclable catalysts with high retention of activity, sometimes higher than that of the free enzyme it was derived from. The enzyme does not need to be of high purity. Indeed, the methodology is essentially a combination of purification and immobilization in one step. The technique is also applicable to the preparation of combi-CLEAs, containing two or more enzymes, for use in one-pot, multi-step synthes...

274 citations

Journal ArticleDOI
TL;DR: A review of the use of enzymes in the textile industry can be found in this paper, covering both current commercial processes and research in this field, including cellulases and laccases.
Abstract: This review highlights the use of enzymes in the textile industry, covering both current commercial processes and research in this field. Amylases have been used for desizing since the middle of the last century. Enzymes used in detergent formulations have also been successfully used over the past 40 years. The application of cellulases for denim finishing and laccases for decolourization of textile effluents and textile bleaching are the most recent commercial advances. New developments rely on the modification of natural and synthetic fibres. Advances in enzymology, molecular biology and screening techniques provide possibilities for the development of new enzyme-based processes for a more environmentally friendly approach in the textile industry.

238 citations

Journal ArticleDOI
TL;DR: Lactobacillus kefir DSM 20587 produces an (R)-specific NADP-dependent alcohol dehydrogenase (ADH) with a broad substrate specificity and a high degree of similarity to short-chain dehydrogenases is indicated.
Abstract: Lactobacillus kefir DSM 20587 produces an (R)-specific NADP-dependent alcohol dehydrogenase (ADH) with a broad substrate specificity. The gene of this ADH was isolated and the complete nucleotide sequence determined. The adh gene comprises 759 bp and encodes a protein of 252 amino acids with a calculated molecular weight of 26 781 Da. The deduced amino acid sequence indicated a high degree of similarity to short-chain dehydrogenases. After cloning and expression in Escherichia coli the enzyme was purified and characterized. For the reduction of acetophenone the specific activity of the homogeneous recombinant ADH was 558 U mg−1. The enzyme shows its maximum activity at 50°C while the pH optimum was at pH 7.0. In order to demonstrate its preparative application, purified ADH was used for the stereoselective reduction of several aliphatic and aromatic ketones as well as β-keto esters. Glucose dehydrogenase was added for the regeneration of NADPH. All prochiral ketones were stereoselectively reduced to the c...

145 citations

Performance
Metrics
No. of papers from the Journal in previous years
YearPapers
202320
202240
202182
202046
201954
201845