scholarly journals Purification and Application of Lipases from Pseudomonas Species

2016 ◽  
Vol 59 (2) ◽  
pp. 111-116
Author(s):  
Saadat Ullah ◽  
Ijaz Malook ◽  
Khair Ul Bashar ◽  
Mehvish Riaz ◽  
Muhammad Mudasar Aslam ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Pseudomonas Aeruginosa ◽  
Substrate Specificity ◽  
Large Scale ◽  
Bacterial Species ◽  
Hydrolytic Enzymes ◽  
Broad Substrate Specificity ◽  
Industrial Sectors ◽  
Pseudomonas Species ◽  
Long Chain

Lipases are important hydrolytic enzymes that hydrolyze long chain triacylglycerol intodiacylglycerol, monoacylglycerol, glycerol and fatty acids. Lipases are found in microorganisms, fungi,plants and animals. Commercially, useful extracellular lipases are isolated from different bacterial species,including Bacillus, Achromobacter, Alcaligenes, Arthrobacter, Pseudomonas, Staphylococcus andChromobacterium species. Among the Pseudomonas species, Pseudomonas aeruginosa, P. cepacia andP. fluorescence are the major producers of lipases. Bacterial lipases have great industrial applicationsbecause of their stability, selectivity and broad substrate specificity. Due to their large scale applicationin industrial sectors, attention is given to isolate Pseudomonas lipases. In this review, purification strategiesfor lipases isolated from Pseudomonas species have been focussed.

scholarly journals Phytophthora infestans Cholinephosphotransferase with Substrate Specificity for Very-Long-Chain Polyunsaturated Fatty Acids

2012 ◽  
Vol 79 (5) ◽  
pp. 1573-1579 ◽  
Author(s):  
Yan Chen ◽  
Hsiang-yun Chi ◽  
Dauenpen Meesapyodsuk ◽  
Xiao Qiu
Keyword(s):  
Fatty Acids ◽  
Substrate Specificity ◽  
Polyunsaturated Fatty Acids ◽  
Phytophthora Infestans ◽  
Neutral Lipids ◽  
Amino Acid Identity ◽  
Pcr Analysis ◽  
Content Type ◽  
Long Chain

ABSTRACTThe effective flux between phospholipids and neutral lipids is critical for a high level of biosynthesis and accumulation of very-long-chain polyunsaturated fatty acids (VLCPUFAs), such as arachidonic acid (ARA; 20:4n-6), eicosapentaenoic acid (EPA; 20:5n-3), and docosahexaenoic acid (DHA; 22:6n-3). Here we describe a cDNA (PiCPT1) fromPhytophthora infestans, a VLCPUFA-producing oomycete, that may have a role in acyl trafficking between diacylglycerol (DAG) and phosphatidylcholine (PC) during the biosynthesis of VLCPUFAs. The cDNA encodes a polypeptide of 393 amino acids with a conserved CDP-alcohol phosphotransferase motif and approximately 27% amino acid identity to theSaccharomyces cerevisiaecholinephosphotransferase (ScCPT1).In vitroassays indicate that PiCPT1 has high cholinephosphotransferase (CPT) activity but no ethanolaminephosphotransferase (EPT) activity. Substrate specificity assays show that it prefers VLCPUFA-containing DAGs, such as ARA DAG and DHA DAG, as substrates. Real-time PCR analysis reveals that expression ofPiCPT1was upregulated inP. infestansorganisms fed with exogenous VLCPUFAs. These results lead us to conclude that PiCPT1 is a VLCPUFA-specific CPT which may play an important role in shuffling VLCPUFAs from DAG to PC in the biosynthesis of VLCPUFAs inP. infestans.

scholarly journals Dietary Fat and Protein Intakes in Relation to Plasma Sphingolipids As Determined by a Large-Scale Lipidomic Analysis

2021 ◽  
Vol 5 (Supplement_2) ◽  
pp. 861-861
Author(s):  
Jowy Seah Yi Hoong ◽  
Wee Siong Chew ◽  
Federico Torta ◽  
Chin Meng Khoo ◽  
Markus R Wenk ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Dietary Fat ◽  
Large Scale ◽  
Saturated Fat ◽  
Dietary Fatty Acids ◽  
Fat Intake ◽  
Polyunsaturated Fat ◽  
Nutrient Intakes ◽  
The Impact ◽  
Long Chain

Abstract Objectives Sphingolipid concentrations have been associated with risk of type 2 diabetes and cardiovascular diseases. Because sphingolipids can be synthesized de novo from saturated fatty acids (SFA), dietary fatty acids may affect plasma sphingolipid concentrations. We aimed to evaluate dietary fat and protein intakes in relation to circulating sphingolipid levels. Methods We used cross-sectional data from 2860 ethnic Chinese Singaporeans collected from 2004–2007. Nutrient intakes were estimated on the basis of a validated 159-item food frequency questionnaire. We quantified 79 molecularly distinct sphingolipids in a large-scale lipidomic evaluation from plasma samples. Results Higher saturated fat intake was associated with higher concentrations of 16:1; O2 sphingolipids including ceramides, monohexosylcermides, dihexosylceramides, sphingomyelins, and sphingosine 1-phosphates. Higher polyunsaturated fat intake was associated with lower plasma long-chain ceramides and long-chain monohexosylcermide concentrations. Protein intake was inversely associated with concentrations of most subclasses of sphingolipids, with the exception of sphingolipids containing a 16:1; O2 sphingoid base. Lower intake of saturated fat and higher intake of polyunsaturated fat and protein may decrease plasma concentrations of several sphingolipid classes. Conclusions These findings may represent a novel biological mechanism for the impact of nutrient intakes on cardio-metabolic health. Funding Sources This work was supported by the National Research Foundation Investigatorship grant (NRF-NRFI2015–05, to MRW), A*STAR (I1901E0040), and the National University Health System (NUHSRO/2014/085/AF-Partner/01, DRH). FT was supported by the NRF and A*STAR IAF-ICP I1901E0040.

scholarly journals Use of an Efflux Pump Inhibitor To Determine the Prevalence of Efflux Pump-Mediated Fluoroquinolone Resistance and Multidrug Resistance in Pseudomonas aeruginosa

2005 ◽  
Vol 49 (2) ◽  
pp. 565-570 ◽  
Author(s):  
Jane Kriengkauykiat ◽  
Edith Porter ◽  
Olga Lomovskaya ◽  
Annie Wong-Beringer
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Multidrug Resistance ◽  
Substrate Specificity ◽  
Efflux Pump ◽  
Fluoroquinolone Resistance ◽  
Cross Resistance ◽  
Broth Microdilution ◽  
Efflux Pump Inhibitor ◽  
Broad Substrate Specificity ◽  
Resistant Strains

ABSTRACT Fluoroquinolone-resistance in Pseudomonas aeruginosa may be due to efflux pump overexpression (EPO) and/or target mutations. EPO can result in multidrug resistance (MDR) due to broad substrate specificity of the pumps. MC-04,124, an efflux pump inhibitor (EPI) shown to significantly potentiate activity of levofloxacin in P. aeruginosa, was used to examine the prevalence of EPO in clinical isolates. MICs were determined for ciprofloxacin, levofloxacin, moxifloxacin, and gatifloxacin with or without EPI and for other antipseudomonal agents by using broth microdilution against P. aeruginosa isolates from adults (n = 119) and children (n = 24). The prevalence of the EPO phenotype (≥8-fold MIC decrease when tested with EPI) was compared among subgroups with different resistance profiles. The EPO phenotype was more prevalent among levofloxacin-resistant than levofloxacin-sensitive strains (61%, 48/79 versus 9%, 6/64). EPO was present in 60% of fluoroquinolone-resistant strains without cross-resistance, while it was present at variable frequencies among strains with cross-resistance to other agents: piperacillin-tazobactam (86%), ceftazidime (76%), cefepime (65%), imipenem (56%), gentamicin (55%), tobramycin (48%), and amikacin (27%). The magnitude of MIC decrease with an EPI paralleled the frequency of which the EPO phenotype was observed in different subgroups. EPI reduced the levofloxacin MIC by as much as 16-fold in eight strains for which MICs were 128 μg/ml. Efflux-mediated resistance appears to contribute significantly to fluoroquinolone resistance and MDR in P. aeruginosa. Our data support the fact that increased fluoroquinolone usage can negatively impact susceptibility of P. aeruginosa to multiple classes of antipseudomonal agents.

scholarly journals Long-Chain Polyunsaturated Fatty Acids Modulate Lung Inflammatory Response Induced by Pseudomonas aeruginosa in Mice

2005 ◽  
Vol 58 (2) ◽  
pp. 211-215 ◽  
Author(s):  
Stéphane Auvin ◽  
François Collet ◽  
Frédéric Gottrand ◽  
Marie-Odile Husson ◽  
Xavier Leroy ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Pseudomonas Aeruginosa ◽  
Inflammatory Response ◽  
Polyunsaturated Fatty Acids ◽  
Long Chain

scholarly journals Polyphenol-Hydroxylating Tyrosinase Activity under Acidic pH Enables Efficient Synthesis of Plant Catechols and Gallols

2021 ◽  
Vol 9 (9) ◽  
pp. 1866
Author(s):  
Hanbit Song ◽  
Pyung-Gang Lee ◽  
Hyun Kim ◽  
Uk-Jae Lee ◽  
Sang-Hyuk Lee ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Large Scale ◽  
Oxidation Reactions ◽  
Plant Polyphenols ◽  
Broad Substrate Specificity ◽  
High Productivity ◽  
Polyphenol Oxidases ◽  
Plant Polyphenol ◽  
Scale Preparation ◽  
Acidic Conditions

Tyrosinase is generally known as a melanin-forming enzyme, facilitating monooxygenation of phenols, oxidation of catechols into quinones, and finally generating biological melanin. As a homologous form of tyrosinase in plants, plant polyphenol oxidases perform the same oxidation reactions specifically toward plant polyphenols. Recent studies reported synthetic strategies for large scale preparation of hydroxylated plant polyphenols, using bacterial tyrosinases rather than plant polyphenol oxidase or other monooxygenases, by leveraging its robust monophenolase activity and broad substrate specificity. Herein, we report a novel synthesis of functional plant polyphenols, especially quercetin and myricetin from kaempferol, using screened bacterial tyrosinases. The critical bottleneck of the biocatalysis was identified as instability of the catechol and gallol under neutral and basic conditions. To overcome such instability of the products, the tyrosinase reaction proceeded under acidic conditions. Under mild acidic conditions supplemented with reducing agents, a bacterial tyrosinase from Bacillus megaterium (BmTy) displayed efficient consecutive two-step monophenolase activities producing quercetin and myricetin from kaempferol. Furthermore, the broad substrate specificity of BmTy toward diverse polyphenols enabled us to achieve the first biosynthesis of tricetin and 3′-hydroxyeriodictyol from apigenin and naringenin, respectively. These results suggest that microbial tyrosinase is a useful biocatalyst to prepare plant polyphenolic catechols and gallols with high productivity, which were hardly achieved by using other monooxygenases such as cytochrome P450s.

Functional characterization of ExFadLO, an outer membrane protein required for exporting oxygenated long-chain fatty acids in Pseudomonas aeruginosa

Biochimie ◽  
2013 ◽  
Vol 95 (2) ◽  
pp. 290-298 ◽  
Author(s):  
Eriel Martínez ◽  
Mónica Estupiñán ◽  
F.I. Javier Pastor ◽  
Montserrat Busquets ◽  
Pilar Díaz ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Functional Characterization ◽  
Long Chain Fatty Acids ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Overview of Recent Advances in Immobilisation Techniques for Phenol Oxidases in Solution

Catalysts ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 467
Author(s):  
Thandanani Ndlovu ◽  
Sidy Ba ◽  
Soraya P Malinga
Keyword(s):  
Substrate Specificity ◽  
Large Scale ◽  
Future Directions ◽  
Enzyme Immobilisation ◽  
Broad Substrate Specificity ◽  
Structural Modifications ◽  
Advantages And Disadvantages ◽  
Phenol Oxidases ◽  
The Past ◽  
Bioremediation Processes

Over the past two decades, phenol oxidases, particularly laccases and tyrosinases, have been extensively used for the removal of numerous pollutants in wastewaters due to their broad substrate specificity and their ability to use readily accessible molecular oxygen as the essential cofactor. As for other enzymes, immobilisation of laccases and tyrosinases has been shown to improve the performance and efficiency of the biocatalysts in solution. Several reviews have addressed the enzyme immobilisation techniques and the application of phenol oxidases to decontaminate wastewaters. This paper offers an overview of the recent publications, mainly from 2012 onwards, on the various immobilisation techniques applied to laccases and tyrosinases to induce and/or increase the performance of the biocatalysts. In this paper, the emphasis is on the efficiencies achieved, in terms of structural modifications, stability and resistance to extreme conditions (pH, temperature, inhibitors, etc.), reactivity, reusability, and broad substrate specificity, particularly for application in bioremediation processes. The advantages and disadvantages of several enzyme immobilisation techniques are also discussed. The relevance and effectiveness of the immobilisation techniques with respect to wastewater decontamination are critically assessed. A perspective on the future directions for large-scale application of the phenol oxidases in immobilised forms is provided.

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