Engineering biocatalytic systems in organic media with low water content

Khmelnitsky, Yu. L.; Levashov, Andrey V.; Klyachko, N. L.; Martínek, Karel

doi:10.1016/0141-0229(88)90115-9

Cited by 325 publications

(90 citation statements)

References 208 publications

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“…The isooctane had a negligible inhibitory effect. The result was somewhat different from that obtained by Khmelnitsky et al (1988). At least thee factors contributed to antimicrobial activity of reverse micelles.…”

Section: Antimicrobial Activity Test Of Four Reverse Micelles and Aotcontrasting

confidence: 54%

Antimicrobial activity of AOT-isooctane reverse micelle as a bioseparation and biocatalysis tool

Chen

Zhao

et al. 2008

Chemical Speciation & Bioavailability

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The antimicrobial activity of different reverse micelles on microorganisms is been compared using the disc diffusion method. The bis (2-ethylhexyl) sodium sulfosuccinate (AOT) reverse micelle showed a more significant inhibitory effect than do other reverse. micelles, and it had an antimicrobial activity against a broad range of microorganisms. Results from an antimicrobial activity test of isooctane and a forward extraction containing soybean protein suggest that the surfactant was chiefly responsible for inhibiting microbes in AOTyisooctane reverse micelle, while isooctane hardly inhibited the microbial growth. The properties of S. aureus, cultured in the TSB with AOT reverse micellar solution, were identified by the SEM and SDS-PAGE fingerprinting of cell-wall proteins. It is concluded that the cellwall of the S. aureus decreased in the TSB with AOT reverse micellar solution, and some cell protein subunits of the S. aureus did not occurr, especially between 14.4 and 42.7 kDa, while one new protein subunit at near 97.4 kDa occurred.

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Section: Antimicrobial Activity Test Of Four Reverse Micelles and Aotcontrasting

confidence: 54%

Antimicrobial activity of AOT-isooctane reverse micelle as a bioseparation and biocatalysis tool

Chen

Zhao

et al. 2008

Chemical Speciation & Bioavailability

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“…The reasons for low activity of protease in organic solvents may be due to limited dispersion of enzymes, the partial denaturation of enzymes and the reduced flexibility of proteins in anhydrous solvents (18). Most of the enzymes are easily inactivated or denatured in organic solvents, and proteases, which are active in organic solvents, have potential application in catalyzing synthetic reactions (15,23). Although all the commercial detergents tested negatively affected the enzyme activity, the enzyme restored a significant 85% activity in the presence of Surf Excel brand of detergent.…”

Section: Resultsmentioning

confidence: 95%

Production of moderately halotolerant, SDS stable alkaline protease from Bacillus cereus MTCC 6840 isolated from lake Nainital, Uttaranchal state, India

Joshi¹,

Kumar²,

Sharma³

2007

Braz. J. Microbiol.

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A moderately cold active, extracellular alkaline protease producing bacterium was isolated from a fresh water lake. The isolate was found to be a gram-positive, rod shaped organism later identified as Bacillus cereus MTCC 6840. The bacterium produced the maximum amount of enzyme when allowed to grow for 24 h at temperature 25º and pH 9.0. Among a variety of substrates used, fructose as a carbon source and a combination of yeast extract and peptone as nitrogen source, supported the maximum protease production by the organism (120 U/ml). Fe ++ and Co ++ stimulated the enzyme activity whereas Ca ++ , Cu ++ , K + , Mg ++ and Mn ++ inhibited it to different extents. The protease was found to be highly stable in the presence of NaCl, SDS and acetone. Treatment with EDTA and PMSF resulted in the considerable loss of enzyme activity. The enzyme was found to be optimally active at pH 9.0 and temperature 20ºC.

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“…All of the purification steps made accordingly by Sisecioglu et al [23][24][25][26] . Fractions of purified enzyme were lyophilized and SDS-PAGE gel electrophoreses used for the checking purity of enzyme 27 ( Figure 1).…”

Section: Purification Of Lpomentioning

confidence: 99%

Inhibition profile of a series of phenolic acids on bovine lactoperoxidase enzyme

Sarıkaya

Şişecioğlu

Çankaya

et al. 2014

Journal of Enzyme Inhibition and Medicinal Chemistry

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Lactoperoxidase (LPO) catalyzes the oxidation of numerous of organic and inorganic substrates by hydrogen peroxide. It has very vital activity in the innate immune system by decreasing or stopping the activation of the bacteria in milk and mucosal secretions. This study's purpose was to investigate in vitro effect of some phenolic acids (ellagic, gallic, ferulic, caffeic, quercetin, p-coumaric, syringic, catechol and epicatechin) on the purified LPO. This enzyme was purified from milk by using different methods such as Amberlite CG-50 resin, CM-Sephadex C-50 ionexchange and Sephadex G-100 gel filtration chromatography. LPO was purified 28.7-fold with a yield of 20.03%. We found phenolic acids have inhibition effects on bovine LPO enzyme to different concentrations. Our study showed lower concentrations of caffeic acid, ferulic acid and quercetin exhibited much higher inhibitory effect on enzyme, so these three of them were clearly a more potent inhibitor than the others were. All of compounds were non-competitive inhibitors.

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Engineering biocatalytic systems in organic media with low water content

Cited by 325 publications

References 208 publications

Antimicrobial activity of AOT-isooctane reverse micelle as a bioseparation and biocatalysis tool

Antimicrobial activity of AOT-isooctane reverse micelle as a bioseparation and biocatalysis tool

Production of moderately halotolerant, SDS stable alkaline protease from Bacillus cereus MTCC 6840 isolated from lake Nainital, Uttaranchal state, India

Inhibition profile of a series of phenolic acids on bovine lactoperoxidase enzyme

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