scholarly journals Cloning, Expression, and Characterization of a Novel Thermostable and Alkaline-stable Esterase from Stenotrophomonas maltophilia OUC_Est10 Catalytically Active in Organic Solvents

Catalysts ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 401 ◽  
Author(s):  
Xinwei Gao ◽  
Xiangzhao Mao ◽  
Ping Lu ◽  
Francesco Secundo ◽  
Changhu Xue ◽  
...  
Keyword(s):  
Organic Solvents ◽  
Stenotrophomonas Maltophilia ◽  
Aqueous Media ◽  
Residual Activity ◽  
Catalytic Triad ◽  
Multiple Sequence ◽  
Medium Temperature ◽  
Reading Frame ◽  
Conserved Sequence ◽  
Catalytically Active

A thermostable and alkaline-stable novel esterase (Est7) was identified through the whole genome sequencing of Stenotrophomonas maltophilia OUC_Est10. The open reading frame of this gene encoded 617 amino acid residues. After heterologous expression in Escherichia coli BL21 (DE3), the purified Est7 was separated as a single protein and presented a molecular mass of 70.6 kDa. Multiple sequence alignment indicated that Est7 had a typical catalytic triad (Ser-Asp-His) and the conserved sequence (GDSL) typical of the family II lipid hydrolase proteins. Est7 showed good stability in alkaline buffers, especially in Tris-HCl buffer at pH 9.0 (residual activity 93.8% after 96 h at 4 °C) and in the medium temperature conditions (residual activity 70.2% after 96 h at 45 °C and pH 8.0). The enzyme also retained higher stability toward several hydrophilic and hydrophobic organic solvents (e.g., after incubation in 100% acetonitrile or in n-hexane the enzyme retained about 97% and 84% of the activity in the absence of organic solvent, respectively). Furthermore, Est7 could catalyze the transesterification reaction of vinylacetate with 2-phenylethanol and cis-3-hexen-1-ol to their corresponding acetate esters in petroleum ether or tert-butyl methyl ether. These results indicate Est7 as a promising biocatalyst for applications of Est7 in non-aqueous media.

scholarly journals Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents

2011 ◽  
Vol 76 (8) ◽  
pp. 1081-1092 ◽  
Author(s):  
Aleksandra Dimitrijevic ◽  
Dusan Velickovic ◽  
Dejan Bezbradica ◽  
Filip Bihelovic ◽  
Ratko Jankov ◽  
...  
Keyword(s):  
Organic Solvents ◽  
Time Course ◽  
Aqueous Media ◽  
Residual Activity ◽  
Nitrogen Sources ◽  
Hydrolytic Activity ◽  
Lipase Production ◽  
Lipase Preparation ◽  
Potential Applications ◽  
Pseudozyma Aphidis

The production of lipase from Pseudozyma aphidis (DSM 70725) was determined in six different media. The highest lipase production was observed in a medium with glucose as the sole carbon source, and yeast extract and sodium nitrate as the nitrogen sources. The time course studies of growth and lipase production in the optimal medium revealed that the highest lipase production was achieved at the end of the log phase of growth, reaching the value of 35.0 U cm-3 in the fifth day of cultivation. The effects of various polar, water-miscible, organic solvents on the activity and stability of the crude lipase produced by P. aphidis were evaluated. The hydrolytic activity of the crude lipase towards p-nitrophenyl palmitate (p-NPP) in aqueous media and in organic solvents was determined, using the same spectrophotometric assay in both the aqueous and organic media. The crude lipase preparation exhibited activity towards p-NPP only in acetone and acetonitrile, while the lipase was stable only in acetone, with 23 % residual activity after 24 h of incubation. These results suggested that lipase from P. aphidis can be used as a biocatalyst for potential applications in such organic solvents.

Transition-Metal-Free Synthetic Strategies for the Cross-Coupling Reactions in Water: A Green Approach

2020 ◽  
Vol 07 ◽  
Author(s):  
Tanmay Chatterjee ◽  
Nilanjana Mukherjee
Keyword(s):  
Transition Metal ◽  
Organic Solvents ◽  
Aqueous Media ◽  
Cross Coupling ◽  
Transition Metal Catalysts ◽  
Synthetic Methods ◽  
Coupling Reactions ◽  
Organic Transformations ◽  
Green Approach ◽  
Dehydrogenative Coupling

Abstract: A natural driving force is always working behind the synthetic organic chemists towards the development of ‘green’ synthetic methodologies for the synthesis of useful classes of organic molecules having potential applications. The majority of the essential classes of organic transformations, including C-C and C-X (X = heteroatom) bond-forming crosscoupling reactions, cross dehydrogenative-coupling (CDC) mostly rely on the requirement of transition-metal catalysts and hazardous organic solvents. Hence, the scope in developing green synthetic strategies by avoiding the use of transitionmetal catalysts and hazardous organic solvents for those important and useful classes of organic transformations is very high. Hence, several attempts are made so far. Water being the most abundant, cheap, and green solvent in the world; numerous synthetic methods have been developed in an aqueous medium. In this review, the development of transitionmetal- free green synthetic strategies for various important classes of organic transformations such as C-C and C-X bondforming cross-coupling, cross dehydrogenative-coupling, and oxidative-coupling in an aqueous media is discussed.

scholarly journals Nitrile Synthesis with Aldoxime Dehydratases: A Biocatalytic Platform with Applications in Asymmetric Synthesis, Bulk Chemicals, and Biorefineries

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4466
Author(s):  
Pablo Domínguez de María
Keyword(s):  
Asymmetric Synthesis ◽  
Organic Solvents ◽  
Raw Materials ◽  
Aqueous Media ◽  
Industrial Processes ◽  
Polymer Chemistry ◽  
Fine Chemicals ◽  
Mild Conditions ◽  
Bulk Chemicals ◽  
Recent Developments

Nitriles comprise a broad group of chemicals that are currently being industrially produced and used in fine chemicals and pharmaceuticals, as well as in bulk applications, polymer chemistry, solvents, etc. Aldoxime dehydratases catalyze the cyanide-free synthesis of nitriles starting from aldoximes under mild conditions, holding potential to become sustainable alternatives for industrial processes. Different aldoxime dehydratases accept a broad range of aldoximes with impressive high substrate loadings of up to >1 Kg L−1 and can efficiently catalyze the reaction in aqueous media as well as in non-aqueous systems, such as organic solvents and solvent-free (neat substrates). This paper provides an overview of the recent developments in this field with emphasis on strategies that may be of relevance for industry and sustainability. When possible, potential links to biorefineries and to the use of biogenic raw materials are discussed.

scholarly journals Iodination of insulin in aqueous and organic solvents

1969 ◽  
Vol 115 (1) ◽  
pp. 11-18 ◽  
Author(s):  
A. Massaglia ◽  
U. Rosa ◽  
G. Rialdi ◽  
C. A. Rossi
Keyword(s):  
Ethylene Glycol ◽  
Organic Solvents ◽  
Molecular Conformation ◽  
Aqueous Media ◽  
Native Structure ◽  
Experimental Conditions ◽  
Polar Environment ◽  
Polar Area ◽  
The Difference ◽  
A Chain

1. The iodination of insulin was studied under various experimental conditions in aqueous media and in some organic solvents, by measuring separately the uptake of iodine by the four tyrosyl groups and the relative amounts of monoiodotyrosine and di-iodotyrosine that are formed. In aqueous media from pH1 to pH9 the iodination occurs predominantly on the tyrosyl groups of the A chain. Some organic solvents increase the iodine uptake of the B-chain tyrosyl groups. Their efficacy in promoting iodination of Tyr-B-16 and Tyr-B-26 is in the order: ethylene glycol and propylene glycol≃methanol and ethanol>dioxan>8m-urea. 2. It is suggested that each of the four tyrosyl groups in insulin has a different environment: Tyr-A-14 is fully exposed to the solvent; Tyr-A-19 is sterically influenced by the environmental structure, possibly by the vicinity of a disulphide interchain bond; Tyr-B-16 is embedded into a non-polar area whose stability is virtually independent of the molecular conformation; Tyr-B-26 is probably in a situation similar to Tyr-B-16 with the difference that its non-polar environment depends on the preservation of the native structure.

Evolutionary History of Plant Lipolytic Enzymes

2018 ◽  
pp. 155-178
Keyword(s):  
Higher Plants ◽  
Evolutionary Relationship ◽  
Biological Evolution ◽  
Sequence Motifs ◽  
Multiple Sequence ◽  
Lipolytic Enzymes ◽  
Conserved Sequence ◽  
Potential Applications ◽  
History Of ◽  
Living Organisms

The discovery of enzymes with lipolytic activities in all kingdoms of life from prokaryote to eukaryote species raises the possibility of the presence of an evolutionary relationship history of these proteins among many species of various living organisms. The chapter suggests a strategy based on the phylogenetic distribution and homology conservation in plant lipolytic enzymes for possible depiction of their biological evolution. Extensive databases and online resources for lipidomics and related areas are useful tools to analyze the different lipolytic enzymes in the three major super kingdoms of life, including higher plants kingdom and confined organisms such as algae that have recently gained much interest due to their promising potential applications in lipids hydrolysis and biosynthesis. Multiple sequence alignments of the identified lipolytic enzymes from databases could serve to the identification of globally conserved residues as well as conserved sequence motifs. Estimation of evolutionary distance between the various identified lipolytic enzymes could also be carried out to better understand the pattern of evolution.

Subsupercritical Water Generated by Inductive Heating Inside Flow Reactors Facilitates the Claisen Rearrangement

Synlett ◽  
2020 ◽  
Vol 31 (19) ◽  
pp. 1942-1946
Author(s):  
Andreas Kirschning ◽  
Mona Oltmanns
Keyword(s):  
Organic Solvents ◽  
High Temperatures ◽  
Claisen Rearrangement ◽  
Flow System ◽  
Aqueous Media ◽  
Inductive Heating ◽  
Flow Conditions ◽  
Flow Reactors

AbstractClaisen rearrangement of electron-deficient O-allylated phenols, including fluorine-modified phenols, is facilitated in aqueous media at high temperatures and pressures under flow conditions, as opposed to organic solvents. The O-allylation of phenols can be coupled with the Claisen rearrangement in an integrated flow system.

Characterization of the Chromosomalaac(6′)-Iz Gene of Stenotrophomonas maltophilia

1999 ◽  
Vol 43 (10) ◽  
pp. 2366-2371 ◽  
Author(s):  
Thierry Lambert ◽  
Marie-Cécile Ploy ◽  
François Denis ◽  
Patrice Courvalin
Keyword(s):  
Stenotrophomonas Maltophilia ◽  
Type I ◽  
Aminoglycoside Resistance ◽  
Reading Frame ◽  
A Value ◽  
Calculated Mass ◽  
Total Dna ◽  
Good Agreement

ABSTRACT The aac(6′)-Iz gene of Stenotrophomonas maltophilia BM2690 encoding an aminoglycoside 6′-N-acetyltransferase was characterized. The gene was identified as a coding sequence of 462 bp corresponding to a protein with a calculated mass of 16,506 Da, a value in good agreement with that of ca. 16,000 found by in vitro coupled transcription-translation. Analysis of the deduced amino acid sequence indicated that the protein was a member of the major subfamily of aminoglycoside 6′-N-acetyltransferases. The enzyme conferred resistance to amikacin but not to gentamicin, indicating that it was an AAC(6′) of type I. The open reading frame upstream from the aac(6′)-Izgene was homologous to the fprA gene of Myxococcus xanthus (61% identity), which encodes a putative pyridoxine (pyridoxamine) 5′-phosphate oxidase. Pulsed-field gel electrophoresis of total DNA from BM2690 and S. maltophilia ATTC 13637 digested with XbaI, DraI, and SpeI followed by hybridization with rRNA and aac(6′)-Iz-specific probes indicated that the gene was located in the chromosome. Theaac(6′)-Iz gene was detected by DNA-DNA hybridization in all 80 strains of S. maltophilia tested. The MICs of gentamicin against these strains of S. maltophilia were lower than those of amikacin, netilmicin, and tobramycin, indicating that production of AAC(6′)-Iz contributes to aminoglycoside resistance in S. maltophilia.

scholarly journals Solvent-controlled E/Z isomerization vs. [2 + 2] photocycloaddition mediated by supramolecular polymerization

2020 ◽  
Vol 11 (38) ◽  
pp. 10405-10413 ◽  
Author(s):  
Torsten Dünnebacke ◽  
Kalathil K. Kartha ◽  
Johannes M. Wiest ◽  
Rodrigo Q. Albuquerque ◽  
Gustavo Fernández
Keyword(s):  
Organic Solvents ◽  
Aqueous Media ◽  
Highly Efficient ◽  
Supramolecular Polymerization

Controlled supramolecular polymerization is used to switch the photoresponsive behaviour of cyanostilbenes from a reversible E/Z photoisomerization in organic solvents to a highly efficient and selective [2 + 2] photocycloaddition in aqueous media.

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