Suitability of non-conventional reaction medium for biocatalysis: From lipase activity to thermophysical characterization

2021 ◽  
Vol 322 ◽  
pp. 114960
Author(s):  
Andrea Fernández ◽  
Laura González ◽  
María S. Álvarez ◽  
Francisco J. Deive
Keyword(s):  
Lipase Activity ◽  
Reaction Medium ◽  
Thermophysical Characterization

Lipase-Catalyzed Acyl-L-Carnitines Synthesis in [Bmim]PF6 Ionic Liquid

2009 ◽  
Vol 5 (1) ◽  
Author(s):  
Jin-qiang Tian ◽  
Qiang Wang ◽  
Zhong-yuan Zhang
Keyword(s):  
Ionic Liquid ◽  
Lipase Activity ◽  
Molecular Sieves ◽  
Reaction Medium ◽  
Molar Ratio ◽  
Reaction Conditions ◽  
Optimal Reaction ◽  
Better Than

In order to significantly improve the biosynthesis of acyl-L-carnitines catalyzed by lipase, there must be an efficient and suitable reaction medium that is not only polar but also hydrophobic. [Bmim]PF6, which satisfies the above two requirements, was applied as the medium. The optimal reaction conditions were: for isovaleryl-L-carnitine, 0.22aW, 200mg molecular sieves, 60ºC, 4:1 of molar ratio (fatty acid:L-carnitine), 150rpm and 60h; for octanoyl-L-carnitine and palmitoyl-L-carnitine, 0.22aW, 250 mg molecular sieves, 5:1 of molar ratio (fatty acid:L-carnitine), 200rpm, 48h, 60ºC (octanoyl-L-carnitine) and 65ºC (palmitoyl-L-carnitine). Their overall yields could reach 59.14%, 90.79% and 98.03%, respectively. The yields of isovaleryl-L-carnitine, octanoyl-L-carnitine and palmitoyl-L-carnitine in [Bmim]PF6 were 16.21%, 73.67% and 44.22 % more than those in acetonitrile, respectively. [Bmim]PF6 as the medium was better than acetonitrile. It could not only enhance the yields of acyl-L-carnitines, but also protect the lipase activity.

ESTIMATION OF LIPASE IN DAIRY PRODUCTS: II. AN EXTRACTION–TITRATION METHOD FOR THE ESTIMATION OF BACTERIAL LIPASE

1949 ◽  
Vol 27f (12) ◽  
pp. 491-498 ◽  
Author(s):  
D. J. Lubert ◽  
L. M. Smith ◽  
H. R. Thornton
Keyword(s):  
Lipase Activity ◽  
Dairy Products ◽  
Skim Milk ◽  
Reaction Medium ◽  
Ether Extract ◽  
Titration Method ◽  
Wide Ph Range ◽  
Ph Range

A method of estimating bacterial lipase is presented that is believed to be more nearly quantitative than any other at present available. The method is based on the titration of acids in an ether extract of a skim milk culture to following a 30 mm period of lipase activity at 37 °C. It is shown that ether-soluble acids carried into the reaction medium do not interfere with the measurements and that ether-soluble acids are not produced from protein or lactose during the test. The method is applicable over a sufficiently wide pH range to make it generally adaptable in bacteriology.

scholarly journals Medium-engineering: a useful tool for modulating lipase activity and selectivity

Biocatalysis ◽  
2016 ◽  
Vol 1 (1) ◽  
Author(s):  
Edmundo Castillo ◽  
Leticia Casas-Godoy ◽  
Georgina Sandoval
Keyword(s):  
Organic Synthesis ◽  
Lipase Activity ◽  
Reaction Medium ◽  
Specific Reaction ◽  
Key Features ◽  
Catalyzed Reactions ◽  
Reaction Media ◽  
Enzymes In Organic Synthesis ◽  
Enhance Activity

AbstractThe design of a specific reaction medium capable to enhance activity, stability, and productivity of biocatalysts has been a recurring topic of study during the last three decades. The remarkable properties and valuable applications of enzymes, especially lipases, have inspiried different strategies for improving their performance in near-anhydrous media. As lipases are the most frequently used enzymes in organic synthesis, understanding the influence of reaction media on their activity and selectivity is crucial. In this paper, we review the key features of lipases and demonstrate how medium-engineering is a useful tool to modulate the activity and selectivity of lipase-catalyzed reactions.

High-voltage cytochemistry for three-dimensional observation of nuclei and calculation of total numbers of nuclear pores in retinal Mueller glia

1990 ◽  
Vol 48 (3) ◽  
pp. 956-957
Author(s):  
H. Ishigooka ◽  
S. Ueno ◽  
L.M. Hjelmeland ◽  
M.B. Landers ◽  
K. Ogawa
Keyword(s):  
Nuclear Envelope ◽  
High Voltage ◽  
Three Dimensional ◽  
Reaction Medium ◽  
Nuclear Pores ◽  
High Voltage Electron Microscopy ◽  
Voltage Electron ◽  
High Voltage Electron ◽  
G6pase Activity ◽  
Mueller Glia

Introduction: We have demonstrated that Glucose-6-phosphatase (G6Pase) activity is localized to the endoplasmic reticulum and nuclear envelope of Mueller glia in the normal and pathological guinea pig retina. Using a combination of this cytochemical technique and high voltage electron microscopy, the distribution of nuclear pores could be clearly observed on the nuclear envelope of Mueller glia because of their anatomical lack of reaction products. This technique was developed to study the three-dimensional structure of nuclei and to calculate total numbers of nuclear pores utilizing a computer graphic analysis system in the normal and pathological retina.Materials and methods: Normal and photocoagulated retina of pigmented adult guinea pigs were perfused with a cold mixture of 0.25% glutaraldehyde and 2% paraformaldehyde in 0.1M cacodylate buffer, and the enucleated globes were hemisected and immersed in the same fixative for 30 min. After sectioning and incubation in the reaction medium for the detection of G6Pase activity by the method of Wachstein-Meisel, the sections were postfixed, dehydrated and embedded in Spurr’s epoxy resin. Serial thick sections (1.0um) were prepared for the observation by a Hitachi high voltage electron microscope (H 1250-M) with an accelerating voltage of 1000 Kv. and pictures were analyzed and three-dimensionally reconstructed by TRI (RATOC Co., Ltd.).

Reaction of Acetaldehyde with Human Platelets

1992 ◽  
Vol 67 (01) ◽  
pp. 126-130 ◽  
Author(s):  
Olivier Spertini ◽  
Jacques Hauert ◽  
Fedor Bachmann
Keyword(s):  
Platelet Aggregation ◽  
Inhibitory Action ◽  
Ex Vivo ◽  
Platelet Rich Plasma ◽  
Shape Change ◽  
Reaction Medium ◽  
Human Platelets ◽  
Membrane Glycoproteins ◽  
Neutral Ph

SummaryPlatelet function defects observed in chronic alcoholics are not wholly explained by the inhibitory action of ethanol on platelet aggregation; they are not completely reproduced either in vivo by short-term ethanol perfusion into volunteers or in vitro by the addition of ethanol to platelet-rich plasma. As acetaldehyde (AcH) binds to many proteins and impairs cellular activities, we investigated the effect of this early degradation product of ethanol on platelets. AcH formed adducts with human platelets at neutral pH at 37° C which were stable to extensive washing, trichloracetic acid hydrolysis and heating at 100° C, and were not reduced by sodium borohydride. The amount of platelet adducts formed was a function of the incubation time and of the concentration of AcH in the reaction medium. At low AcH concentrations (<0.2 mM), platelet bound AcH was directly proportional to the concentration of AcH in the reaction medium. At higher concentrations (≥0.2 mM), AcH uptake by platelets tended to reach a plateau. The amount of adducts was also proportional to the number of exposures of platelets to pulses of 20 pM AcH.AcH adducts formation severely impaired platelet aggregation and shape change induced by ADP, collagen and thrombin. A positive correlation was established between platelet-bound AcH and inhibition of aggregation.SDS-PAGE analysis of AcH adducts at neutral pH demonstrated the binding of [14C]acetaldehyde to many platelet proteins. AcH adduct formation with membrane glycoproteins, cytoskeleton and enzymes might interfere with several steps of platelet activation and impair platelet aggregation.This in vitro study shows that AcH has a major inhibitory action on platelet aggregation and may account for the prolonged ex vivo inhibition of aggregation observed in chronic alcoholics even in the absence of alcoholemia.

Chemical Transformation of Fe, Air & Water to Ammonia: Variation of Reaction Rate with Temperature, Pressure, Alkalinity and Iron

2018 ◽  
Author(s):  
Ping Peng ◽  
Fang-Fang Li ◽  
Xinye Liu ◽  
Jiawen Ren ◽  
jessica stuart ◽  
...  
Keyword(s):  
Particle Size ◽  
Reaction Rate ◽  
Electrolyte Concentration ◽  
Iron Concentration ◽  
Reaction Medium ◽  
Iron Particle ◽  
Intermediate Step ◽  
Ammonia Production ◽  
Pure Nitrogen ◽  
Alkaline Reaction

The rate of ammonia production by the <u>chemical </u>oxidation of iron, N<sub>2</sub>(from air or as pure nitrogen) and water is studied as a function of (1) iron particle size, (2) iron concentration, (3) temperature, (4) pressureand (5) concentration of the alkaline reaction medium. The reaction meduium consists of an aqueous solution of equal molal concentrations of NaOH and KOH (Na<sub>0.5</sub>K<sub>0.5</sub>OH). We had previously reported on the <u>chemical </u>reaction of iron and nitrogen in alkaline medium to ammonia as an intermediate step in the <u>electrochemical </u>synthesis of ammonia by a nano-sized iron oxide electrocatlyst. Here, the intermediate <u>chemical </u>reaction step is exclusively explored. The ammonia production rate increases with temperature (from 20 to 250°C), pressure (from 1 atm to 15 atm of air or N<sub>2</sub>), and exhibits a maximum rate at an electrolyte concentration of 8 molal Na<sub>0,5</sub>K<sub>0,5</sub>OH in a sealed N<sub>2</sub>reactor. 1-3 µm particle size Fe drive the highest observed ammonia production reaction rate. The Fe mass normalized rate of ammonia production increases with decreasing added mass of the Fe reactant reaching a maximum observed rate of 2.2x10<sup>-4</sup>mole of NH<sub>3</sub>h<sup>-1</sup>g<sup>-1</sup>for the reaction of 0.1 g of 1-3 µm Fe in 200°C 8 molal Na<sub>0.5</sub>K<sub>0.5</sub>OH at 15 atm. Under these conditions 5.1 wt% of the iron reacts to form NH<sub>3</sub>via the reaction N<sub>2</sub>+ 2Fe + 3H<sub>2</sub>O ®2NH<sub>3</sub>+ Fe<sub>2</sub>O<sub>3</sub>.

Bio-PCM thermophysical characterization through the T-history method

2017 ◽  
Author(s):  
Lucas Lira ◽  
Mariana Moronari Monteiro ◽  
Antonio Brasil Junior ◽  
Taygoara Oliveira
Keyword(s):  
Thermophysical Characterization
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