Game Theory

HernÃ¡ndez, PenÃ©lope; Pavan, Marina

doi:10.1057/9781137538192.0008

Cited by 8 publications

(11 citation statements)

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“…The basic biochemical properties of L. reuteri 121 Inu are comparable to those reported for levansucrase enzymes of S. salivarius and G. diazotrophicus (Table 2). These levansucrase enzymes all display Michaelis^Menten type of kinetics for the [7]. c Data from [8].…”

Section: Discussionmentioning

confidence: 99%

“…The Inu enzyme from L. reuteri 121 produced large amounts of the fructo-oligosaccharide 1-kestose. 1-Kestose production has been reported with FTFs from Paenibacillus polymyxa CF43 [19], G. diazotrophicus SRT4 [7], and Zymomonas mobilis ATCC 10988 [20]. Interestingly, the main products of these enzymes are levan polymers with L(2C6) linked fructosyl units.…”

Section: Discussionmentioning

confidence: 99%

“…2.4.1.10), synthesizing levan polymers with L(2C6) linked fructosyl units, occur more widespread in bacteria and have been studied in more detail. The biochemical characteristics of the levansucrases from Bacillus subtilis [6], Gluconacetobacter diazotrophicus [7], and Streptococcus salivarius [8] have been determined. These studies have shown that levansucrase enzymes display Michaelis^Menten type of kinetics for the transferase and hydrolysis reactions.…”

Section: Introductionmentioning

confidence: 99%

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Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

2002

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Inulosucrases catalyze transfer of a fructose moiety from sucrose to a water molecule (hydrolysis) or to an acceptor molecule (transferase), yielding inulin. Bacterial inulin production is rare and a biochemical analysis of inulosucrase enzymes has not been reported. Here we report biochemical characteristics of a puri¢ed recombinant inulosucrase enzyme from Lactobacillus reuteri. It displayed Michaelis^Menten type of kinetics with substrate inhibition for the hydrolysis reaction. Kinetics of the transferase reaction is best described by the Hill equation, not reported before for these enzymes. A C-terminal deletion of 100 amino acids did not appear to a¡ect enzyme activity or product formation. This truncated form of the enzyme was used for biochemical characterization.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

2002

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“…Whether sPLA 2 activity is actually required for GIVA PLA 2 activation (i.e. whether or not sPLA 2 acts on a speci¢c surface receptor) is a matter of debate and probably depends on the type of cell that interacts with the exogenous enzyme [30,32,33].…”

Section: Pla 2 and Aa Releasementioning

confidence: 99%

Phospholipase A₂ regulation of arachidonic acid mobilization

2002

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Phospholipase A 2 (PLA 2 ) constitutes a growing superfamily of lipolytic enzymes, and to date, at least 19 distinct enzymes have been found in mammals. This class of enzymes has attracted considerable interest as a pharmacological target in view of its role in lipid signaling and its involvement in a variety of in£ammatory conditions. PLA 2 s hydrolyze the sn-2 ester bond of cellular phospholipids, producing a free fatty acid and a lysophospholipid, both of which are lipid signaling molecules. The free fatty acid produced is frequently arachidonic acid (AA,5,8,11,, the precursor of the eicosanoid family of potent in£ammatory mediators that includes prostaglandins, thromboxanes, leukotrienes and lipoxins. Multiple PLA 2 enzymes are active within and surrounding the cell and these enzymes have distinct, but interconnected roles in AA release.

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“…Classical microbiological methods for determining antimicrobial compounds in feeds are time consuming and nonspecific, and moreover, both bioassay and TLC methods were not capable of exact quantitation. CE (HPCE) has been widely used for analysis of antibiotics in biological samples, but little has been reported concerning feed samples [20]. The only relevant article concerning detection of TCs or MALs in feeds by CE was a report by Hernández that measured DOC and OTC in feedstuffs using micellar electrokinetic capillary chromatography [21].…”

Section: Introductionmentioning

confidence: 99%

Simultaneous determination of five tetracycline and macrolide antibiotics in feeds using HPCE

Tong¹,

Rao²,

Zhu³

et al. 2009

J of Separation Science

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This work demonstrates the potential of HPCE in the analysis of antibiotics in a complex matrix such as feedstuffs. Using 20 mM citric acid-40 mM Na 2 HPO 4 buffer (pH 2.65), the five antibiotics, tetracycline, oxytetracycline, doxycycline, tilmicosin, and tylosin were successfully separated at 30 kV in a 64.5 cm Â 75 mm id capillary. Good repeatability, stability, and reliability of the method were supported by o10% CV with mean recoveries of 470%, and the limit of detection of the five analytes was 0.5-1 mg/kg. It was for the first time that a capillary electrophoretic method was employed to simultaneously detect five tetracycline and macrolide antibiotics in animal feeds.

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Game Theory

Cited by 8 publications

References 0 publications

Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

Phospholipase A₂ regulation of arachidonic acid mobilization

Simultaneous determination of five tetracycline and macrolide antibiotics in feeds using HPCE

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Game Theory

Cited by 8 publications

References 0 publications

Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

Phospholipase A2 regulation of arachidonic acid mobilization

Simultaneous determination of five tetracycline and macrolide antibiotics in feeds using HPCE

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Product

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Phospholipase A₂ regulation of arachidonic acid mobilization