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Journal articles on the topic 'Lactones; Catalysis; Biocatalysis'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Kwon, Seok Joon, Heung-Chae Jung та Jae-Gu Pan. "Transgalactosylation in a Water-Solvent Biphasic Reaction System with β-Galactosidase Displayed on the Surfaces of Bacillus subtilis Spores". Applied and Environmental Microbiology 73, № 7 (2006): 2251–56. http://dx.doi.org/10.1128/aem.01489-06.

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ABSTRACT The ever-increasing industrial demand for biocatalysis necessitates innovations in the preparation and stabilization of biocatalysts. In this study, we demonstrated that β-galactosidase (β-Gal) displayed on Bacillus spores by fusion to the spore coat proteins (CotG) may be used as a whole-cell immobilized biocatalyst for transgalactosylation in water-solvent biphasic reaction systems. The resulting spores had a specific hydrolytic activity of 5 × 103 U/g (dry weight) of spores. The β-Gal was tightly attached to the spore surface and was more stable in the presence of various organic s

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Szelwicka, Anna, Anna Kolanowska, Piotr Latos, Sebastian Jurczyk, Slawomir Boncel та Anna Chrobok. "Carbon nanotube/PTFE as a hybrid platform for lipase B from Candida antarctica in transformation of α-angelica lactone into alkyl levulinates". Catalysis Science & Technology 10, № 10 (2020): 3255–64. http://dx.doi.org/10.1039/d0cy00545b.

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Martin, Collin H., Danyi Wu, and Kristala L. Jones Prather. "Integrated Bioprocessing for the pH-Dependent Production of 4-Valerolactone from Levulinate in Pseudomonas putida KT2440." Applied and Environmental Microbiology 76, no. 2 (2009): 417–24. http://dx.doi.org/10.1128/aem.01769-09.

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ABSTRACT Enzymes are powerful biocatalysts capable of performing specific chemical transformations under mild conditions, yet as catalysts they remain subject to the laws of thermodynamics, namely, that they cannot catalyze chemical reactions beyond equilibrium. Here we report the phenomenon and application of using extracytosolic enzymes and medium conditions, such as pH, to catalyze metabolic pathways beyond their intracellular catalytic limitations. This methodology, termed “integrated bioprocessing” because it integrates intracellular and extracytosolic catalysis, was applied to a lactoniz

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Moreno-Horn, Marcus, Enriqueta Martinez-Rojas, Helmut Görisch, Roland Tressl та Leif Alexander Garbe. "Oxidation of 1,4-alkanediols into γ-lactones via γ-lactols using Rhodococcus erythropolis as biocatalyst". Journal of Molecular Catalysis B: Enzymatic 49, № 1-4 (2007): 24–27. http://dx.doi.org/10.1016/j.molcatb.2007.07.004.

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5

Zhang, Qiu-Hua, Liu Yang, Yi-Bin Tang, Liu-Nv Huang, and Wen-Fang Luo. "Industrial kinetic resolution of d,l-pantolactone by an immobilized whole-cell biocatalyst." RSC Advances 11, no. 48 (2021): 30373–76. http://dx.doi.org/10.1039/d1ra05708a.

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Immobilized whole-cells of Pichia pastoris harboring recombinant d-lactonase were entrapped in calcium alginate gels and used as an efficient biocatalyst for catalytic kinetic resolution of d,l-pantolactone.

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6

Grabarczyk, Małgorzata, Wanda Mączka, Katarzyna Wińska, et al. "Pleurotus ostreatus as a Biocatalyst to Obtain Bicyclic Hydroxylactones with Three or Four Methyl Groups." Catalysts 9, no. 8 (2019): 643. http://dx.doi.org/10.3390/catal9080643.

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The purpose of the study was to explore microbial transformations in cultures of basidiomycetes Pleurotus ostreatus, two bicyclic unsaturated lactones occurring in the form of two diastereoisomers. Some of these strains were able to transform unsaturated lactones into four known and three new derivatives. The structures of all lactones were established on the basis of spectroscopic data. Both substrates and products caused a complete inhibition of growth of A. alternata and F. linii strains.

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Mazur, Marcelina, Anna Kudrynska, Aleksandra Pawlak, Beatriz Hernandez-Suarez, Bożena Obmińska-Mrukowicz, and Witold Gładkowski. "Biotechnological Approach for the Production of Enantiomeric Hydroxylactones Derived from Benzaldehyde and Evaluation of Their Cytotoxic Activity." Catalysts 10, no. 11 (2020): 1313. http://dx.doi.org/10.3390/catal10111313.

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The β-aryl-δ-halo-γ-lactones are known for their antiproliferative activity towards numerous cancer cell lines. The aim of this study was to obtain in the biotransformation process new β-aryl-δ-hydroxy-γ-lactones and compare their activity with the antiproliferative activity of parent compounds. The racemic cis-5-(1-iodoethyl)-4-phenyldihydrofuran-2-one as well as separate enantiomers were transformed in fungal cultures. Among ten tested biocatalysts, three (Absidia cylindrospora AM336, Absidia glauca AM254, and Fusarium culmorum AM10) were able to catalyze the hydrolytic dehalogenation proces

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Castejón-Vilatersana, Mireia, Magda Faijes, and Antoni Planas. "Transglycosylation Activity of Engineered Bifidobacterium Lacto-N-Biosidase Mutants at Donor Subsites for Lacto-N-Tetraose Synthesis." International Journal of Molecular Sciences 22, no. 6 (2021): 3230. http://dx.doi.org/10.3390/ijms22063230.

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The health benefits of human milk oligosaccharides (HMOs) make them attractive targets as supplements for infant formula milks. However, HMO synthesis is still challenging and only two HMOs have been marketed. Engineering glycoside hydrolases into transglycosylases may provide biocatalytic routes to the synthesis of complex oligosaccharides. Lacto-N-biosidase from Bifidobacterium bifidum (LnbB) is a GH20 enzyme present in the gut microbiota of breast-fed infants that hydrolyzes lacto-N-tetraose (LNT), the core structure of the most abundant type I HMOs. Here we report a mutational study in the

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9

Misson, Mailin, Bo Jin, Sheng Dai та Hu Zhang. "Interfacial Biocatalytic Performance of Nanofiber-Supported β-Galactosidase for Production of Galacto-Oligosaccharides". Catalysts 10, № 1 (2020): 81. http://dx.doi.org/10.3390/catal10010081.

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Molecular distribution, structural conformation and catalytic activity at the interface between enzyme and its immobilising support are vital in the enzymatic reactions for producing bioproducts. In this study, a nanobiocatalyst assembly, β-galactosidase immobilized on chemically modified electrospun polystyrene nanofibers (PSNF), was synthesized for converting lactose into galacto-oligosaccharides (GOS). Characterization results using scanning electron microscopy (SEM) and fluorescence analysis of fluorescein isothiocyanat (FITC) labelled β-galactosidase revealed homogenous enzyme immobilizat

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10

Feske, Brent, Sarah Franz, Richard Watkins та ін. "Synthetic Strategy toward γ-Keto Nitriles and Their Biocatalytic Conversion to Asymmetric γ-Lactones". Synthesis 45, № 15 (2013): 2171–78. http://dx.doi.org/10.1055/s-0033-1339282.

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11

Karmee, Sanjib Kumar, Bernd Niemeijer, Laura Casiraghi, Benhilda Mlambo, Alexei Lapkin, and Lasse Greiner. "Facile biocatalytic synthesis of a macrocyclic lactone in sub- and supercritical solvents." Biocatalysis and Biotransformation 32, no. 2 (2014): 125–31. http://dx.doi.org/10.3109/10242422.2014.893579.

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12

Zaidan, Uswatun Hasanah, Mohd Basyaruddin Abdul Rahman, Siti Salhah Othman, et al. "Biocatalytic production of lactose ester catalysed by mica-based immobilised lipase." Food Chemistry 131, no. 1 (2012): 199–205. http://dx.doi.org/10.1016/j.foodchem.2011.08.060.

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13

Schrittwieser, Joerg, Stefan Velikogne та Wolfgang Kroutil. "Artificial Biocatalytic Linear Cascades to Access Hydroxy Acids, Lactones, and α- and β-Amino Acids". Catalysts 8, № 5 (2018): 205. http://dx.doi.org/10.3390/catal8050205.

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α-, β-, and ω-Hydroxy acids, amino acids, and lactones represent common building blocks and intermediates for various target molecules. This review summarizes artificial cascades published during the last 10 years leading to these products. Renewables as well as compounds originating from fossil resources have been employed as starting material. The review provides an inspiration for new cascade designs and may be the basis to design variations of these cascades starting either from alternative substrates or extending them to even more sophisticated products.

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14

Czyzewska, Katarzyna, and Anna Trusek. "Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature." Catalysts 11, no. 5 (2021): 527. http://dx.doi.org/10.3390/catal11050527.

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The current requirements of industrial biocatalysis are related to economically beneficial and environmentally friendly processes. Such a strategy engages low-temperature reactions. The presented approach is essential, especially in food processes, where temperature affects the quality and nutritional value foodstuffs. The subject of the study is the hydrolysis of lactose with the commercial lactase NOLA™ Fit 5500 (NOLA). The complete decomposition of lactose into two monosaccharides gives a sweeter product, recommended for lactose intolerant people and those controlling a product’s caloric co

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15

Todea, Anamaria, Linda G. Otten, August E. Frissen, Isabel W. C. E. Arends, Francisc Peter, and Carmen G. Boeriu. "Selectivity of lipases for estolides synthesis." Pure and Applied Chemistry 87, no. 1 (2015): 51–58. http://dx.doi.org/10.1515/pac-2014-0716.

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AbstractLipase-catalyzed synthesis of estolides starting from different saturated (C16 16OH, C18 12OH) and unsaturated (C18:1 9 cis 12-OH) hydroxy-fatty acids was investigated. For this reason, the catalytic efficiency of several native and immobilized lipases in different organic reaction media at temperatures up to 75 °C was studied. The formation of mono- and di-lactone as well as estolide’s chain elongation depends on the type and source of lipase. The lipase from Pseudomonas stutzeri immobilized by cross-linking as cross-linked enzymes aggregates (CLEAs) was the best biocatalyst in terms

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16

Ferreira-Torres, C., M. Micheletti, and G. J. Lye. "Microscale process evaluation of recombinant biocatalyst libraries: application to Baeyer–Villiger monooxygenase catalysed lactone synthesis." Bioprocess and Biosystems Engineering 28, no. 2 (2005): 83–93. http://dx.doi.org/10.1007/s00449-005-0422-4.

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17

Mahadevaiah, Shilpa, Renuka Basavaiah, Manmohan Parida та Harsh Vardhan Batra. "Optimal Production of β-Galactosidase from Lactobacillus fermentum for the Synthesis of Prebiotic Galactooligosaccharides (Gos)". Journal of Pure and Applied Microbiology 14, № 4 (2020): 2769–80. http://dx.doi.org/10.22207/jpam.14.4.53.

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The enzyme β-galactosidase (β-gal) has extensively used for improvement of lactose intolerance condition. Present study, was designed to assess the potential of β-gal enzyme produced by Lactobacillus fermentum, a kefir isolate, as a biocatalyst for the manufacture of prebiotic galactooligosaccharides (GOS) from lactose. The efficiency of L. fermentum to produce β-gal of 4,254 u/ml was determined by permeabilizing the cells with solvents such as sodium dodecyl sulfate (SDS) and chloroform. Different parameters contributing β-gal production including reaction time, temperature, pH, carbohydrates

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18

Kamerbeek, Nanne M., Arjen J. J. Olsthoorn, Marco W. Fraaije, and Dick B. Janssen. "Substrate Specificity and Enantioselectivity of 4-Hydroxyacetophenone Monooxygenase." Applied and Environmental Microbiology 69, no. 1 (2003): 419–26. http://dx.doi.org/10.1128/aem.69.1.419-426.2003.

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ABSTRACT The 4-hydroxyacetophenone monooxygenase (HAPMO) from Pseudomonas fluorescens ACB catalyzes NADPH- and oxygen-dependent Baeyer-Villiger oxidation of 4-hydroxyacetophenone to the corresponding acetate ester. Using the purified enzyme from recombinant Escherichia coli, we found that a broad range of carbonylic compounds that are structurally more or less similar to 4-hydroxyacetophenone are also substrates for this flavin-containing monooxygenase. On the other hand, several carbonyl compounds that are substrates for other Baeyer-Villiger monooxygenases (BVMOs) are not converted by HAPMO.

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19

Rustoy, Eduardo M., Elba N. Pereyra, Silvia Moreno, and Alicia Baldessari. "Combination strategy using pure enzymes and whole cells as biocatalysts for the preparation of 2-hydroxyesters and lactones from 2-oxoglutaric acid." Tetrahedron: Asymmetry 15, no. 23 (2004): 3763–68. http://dx.doi.org/10.1016/j.tetasy.2004.10.013.

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20

EREMIA, MIHAELA CARMEN, and MARIA-MONICA PETRESCU. "Production, purification and immobilization of inulinases from Aspergillius species." Romanian Biotechnological Letters 26, no. 3 (2021): 2685–91. http://dx.doi.org/10.25083/rbl/26.3/2685-2691.

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Inulinases are enzymes catalysing hydrolysis of polyfructosans to produce fructose or fructooligosaccharides; these properties have attracted interest of many researchers towards exploring various plant sources (agro food waste) as substrates. According to the literature, various microorganisms, such as fungi, yeast, bacteria, and actinomycetes, can synthesize inulinase. Producer microorganisms can be the micromycetes Aspergillus, Penicillium, Rhizopus and Fusarium, the yeast Kluyveromyces and the bacteria Clostridium thermosuccinogenes and Bacillus subtilis, using inulin, sucrose, fructose, l

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21

Iwaki, Hiroaki, Shaozhao Wang, Stephan Grosse, et al. "Pseudomonad Cyclopentadecanone Monooxygenase Displaying an Uncommon Spectrum of Baeyer-Villiger Oxidations of Cyclic Ketones." Applied and Environmental Microbiology 72, no. 4 (2006): 2707–20. http://dx.doi.org/10.1128/aem.72.4.2707-2720.2006.

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ABSTRACT Baeyer-Villiger monooxygenases (BVMOs) are biocatalysts that offer the prospect of high chemo-, regio-, and enantioselectivity in the organic synthesis of lactones or esters from a variety of ketones. In this study, we have cloned, sequenced, and overexpressed in Escherichia coli a new BVMO, cyclopentadecanone monooxygenase (CpdB or CPDMO), originally derived from Pseudomonas sp. strain HI-70. The 601-residue primary structure of CpdB revealed only 29% to 50% sequence identity to those of known BVMOs. A new sequence motif, characterized by a cluster of charged residues, was identified

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22

Nesrine, Lenchi, Kebbouche Salima, Khelfaoui Mohamed Lamine, et al. "Phylogenetic characterization and screening of halophilic bacteria from Algerian salt lake for the production of biosurfactant and enzymes." World Journal of Biology and Biotechnology 5, no. 2 (2020): 1. http://dx.doi.org/10.33865/wjb.005.02.0294.

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Environments containing significant concentration of NaCl such as salt lakes harbor extremophiles microorganisms which have a great biotechnology interest. To explore the diversity of Bacteria in Chott Tinsilt (Algeria), an isolation program was performed. Water samples were collected from the saltern during the pre-salt harvesting phase. This Chott is high in salt (22.47% (w/v). Seven halophiles Bacteria were selected for further characterization. The isolated strains were able to grow optimally in media with 10–25% (w/v) total salts. Molecular identification of the isolates was performed by

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23

Castagnolo, Daniele, Fei Zhao, Domiziana Masci, and Elena Tomarelli. "Biocatalytic and Chemo-Enzymatic Approaches for the Synthesis of Heterocycles." Synthesis, July 28, 2020. http://dx.doi.org/10.1055/s-0040-1707210.

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Heterocycles are ubiquitous structures in nature and can be found in many drugs and chemicals. Biocatalysts, alone or in combination with other metal catalysts, can be exploited for the construction of various heterocyclic rings under mild reaction conditions. This Short Review highlights the recent advances in the development of biocatalytic and chemo-enzymatic methods for the synthesis of both aliphatic and aromatic heterocyclic rings.1 Introduction2 Synthesis of Aliphatic Heterocycles2.1 Piperidines, Pyrrolidines and Piperazines2.2 Other Nitrogen-Containing Aliphatic Heterocycles2.3 Lactone

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24

Liu, Yuan-Yang, Chun-Xiu Li, Jian-He Xu, and Gao-Wei Zheng. "Efficient Synthesis of Methyl 3-Acetoxypropionate by a Newly Identified Baeyer-Villiger Monooxygenase." Applied and Environmental Microbiology 85, no. 11 (2019). http://dx.doi.org/10.1128/aem.00239-19.

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ABSTRACT Baeyer-Villiger monooxygenases (BVMOs) are an emerging class of promising biocatalysts for the oxidation of ketones to prepare corresponding esters or lactones. Although many BVMOs have been reported, the development of highly efficient enzymes for use in industrial applications is desirable. In this work, we identified a BVMO from Rhodococcus pyridinivorans (BVMORp) with a high affinity toward aliphatic methyl ketones (Km < 3.0 μM). The enzyme was highly soluble and relatively stable, with a half-life of 23 h at 30°C and pH 7.5. The most effective substrate discovered so far is 2-

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25

Xie, Linan, Dongliang Xiao, Xiaojing Wang, et al. "Combinatorial Biosynthesis of Sulfated Benzenediol Lactones with a Phenolic Sulfotransferase from Fusarium graminearum PH-1." mSphere 5, no. 6 (2020). http://dx.doi.org/10.1128/msphere.00949-20.

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ABSTRACT Total biosynthesis or whole-cell biocatalytic production of sulfated small molecules relies on the discovery and implementation of appropriate sulfotransferase enzymes. Although fungi are prominent biocatalysts and have been used to sulfate drug-like phenolics, no gene encoding a sulfotransferase enzyme has been functionally characterized from these organisms. Here, we identify a phenolic sulfotransferase, FgSULT1, by genome mining from the plant-pathogenic fungus Fusarium graminearum PH-1. We expressed FgSULT1 in a Saccharomyces cerevisiae chassis to modify a broad range of benzenedi

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26

Dorau, Robin, Lin Chen, Jianming Liu, Peter Ruhdal Jensen та Christian Solem. "Efficient production of α-acetolactate by whole cell catalytic transformation of fermentation-derived pyruvate". Microbial Cell Factories 18, № 1 (2019). http://dx.doi.org/10.1186/s12934-019-1271-1.

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Abstract Background Diacetyl provides the buttery aroma in products such as butter and margarine. It can be made via a harsh set of chemical reactions from sugarcane bagasse, however, in dairy products it is normally formed spontaneously from α-acetolactate, a compound generated by selected lactic acid bacteria in the starter culture used. Due to its bacteriostatic properties, it is difficult to achieve high levels of diacetyl by fermentation. Here we present a novel strategy for producing diacetyl based on whole-cell catalysis, which bypasses the toxic effects of diacetyl. Results By expressi

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"Advanced Biocatalysts Based on Hexahistidine-Containing organophosphorus Hydrolase for Chemical and Biological Defense." Journal of NBC Protection Corps 3, no. 2 (2019): 111–16. http://dx.doi.org/10.35825/2587-5728-2019-3-2-111-116.

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The advanced biocatalysts based on hexahistidine-tagged organophosphorus hydrolase (His6-OPH) were recently developed for the detoxification of various organophosphorus compounds and degradation of N-acyl homoserine lactones. Due to enzyme immobilization, some of obtained biocatalysts are quite stable, easy to use and very effective/active (e.g. tens of millions of substrate solution volumes appeared to be treated with column cartridges containing immobilized His6-OPH). Recently, the possible bioengineering of different stabilized nanocomplexes of His6-OPH due to its non-covalent binding with

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28

Bednarski, W., та A. Kulikowska. "Influence of two-phase system composition on biocatalytic properties of β-galactosidase preparations". Chemical Papers 61, № 5 (2007). http://dx.doi.org/10.2478/s11696-007-0049-9.

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AbstractA comparison was made between the catalytic properties of β-galactosidase from Penicillium canescens and Aspergillus oryzae using lactose in two-phase systems of an organic solvent and water. It was shown that the ability of β-galactosidase preparations to synthesize galactooligosaccharides depends on the type of the solvent used (cyclohexane, hexane, toluene) and on its proportion in the two-phase system. The use of cyclohexane in the reaction medium stabilized the activity of β-galactosidase from P. canescens which was immobilized on tosylated cotton cloth, and enabled its multiple u

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Todea, Anamaria, Ioana Cristina Benea, Ioan Bîtcan та ін. "One-pot biocatalytic conversion of lactose to gluconic acid and galacto-oligosaccharides using immobilized β-galactosidase and glucose oxidase". Catalysis Today, серпень 2020. http://dx.doi.org/10.1016/j.cattod.2020.06.090.

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