Application of Alkaline Phosphatases from Different Sources in Pharmaceutical and Clinical Analysis for the Determination of Their Cofactors; Zinc and Magnesium Ions

Muginova, S. V.; Zhavoronkova, A. M.; Polyakov, Alexei E.; Шеховцова, Т. Н.

doi:10.2116/analsci.23.357

Cited by 22 publications

(13 citation statements)

References 23 publications

(25 reference statements)

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“…Alkaline phosphatase (ALP) is a hydrolase enzyme that removes phosphate groups from many kinds of molecules (EC3.1.3.1) and can be obtained from various sources [Muginova et al, 2007]. ALP can be used in different fields such as immunoassays and electrochemical immunosensors as a labeling enzyme in the dairy industry as an indicator of successful pasteurization, in molecular biology laboratories for preserving DNA molecules, etc.…”

Section: Introductionmentioning

confidence: 99%

“…ALP can be used in different fields such as immunoassays and electrochemical immunosensors as a labeling enzyme in the dairy industry as an indicator of successful pasteurization, in molecular biology laboratories for preserving DNA molecules, etc. (Muginova et al, 2007;Kreuzer et al, 1999;Rankin et al, 2010;Rittie and Perbal, 2008). Therefore, the improvement of the enzymatic functional stability is important.…”

Section: Introductionmentioning

confidence: 99%

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Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Jafary

Panjehpour

Varshosaz

et al. 2016

Braz. J. Chem. Eng.

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-Enzyme engineering via immobilization techniques is a suitable approach for improving enzyme function and stability and is superior to the other chemical or biological methods. In this study chitosan nanoparticles were synthesized using the Ionic Gelation method and were characterized by Fourier Transform Infrared Spectroscopy (FTIR), Scanning Electron Microscopy (SEM) and Transmission Electron Microscopy (TEM). Alkaline phosphatase was successfully immobilized on the chitosan nanoparticles in optimum conditions. Chitosan nanoparticles were used because of their special properties for enzyme immobilization. This study indicated that the immobilized enzyme has improved function at high temperature and during storage. Immobilization resulted in an increased range of optimum pH and temperature, and reusability of enzyme. Furthermore, the binding efficiency calculation indicated that the immobilized alkaline phosphatase conserved 71% of its native activity. Kinetic parameter studies indicated no significant difference between the immobilized and free enzymes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Jafary

Panjehpour

Varshosaz

et al. 2016

Braz. J. Chem. Eng.

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“…Besides its effect on human health problem, ALP are usefully applied in various fields such as molecular research tool as well as enzyme immunoassays especially bacterial alkaline phosphatase (Dong & Zeikus, 1997;Sun et al, 2007). ), milk industry for validation of milk pasteurization (Rankin et al, 2010), cosmetics as a substance for the regeneration and metabolism of cells, environment for monitoring herbicides or pesticides (Muginova et al, 2007), clinical diagnosis as a marker and medicine such as calf intestinal alkaline phosphates, a therapeutic drug for lipopolysaccharide-mediated diseases (Beumer et al, 2003). Despite its wide application, ALP with greater activity or novel properties suitable for commercial applications is still required such as ALP which is active under the high salt concentration and high thermal stability or storage stability.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Alkaline Phosphatase Producing Bacteria Isolated from Thai Fermented Fish Products

Sitdhipol¹,

Niwasabutra²,

Wannissorn³

et al. 2012

IJB

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Seventeen isolates of alkaline phosphatase (ALP) producing bacteria were screened and systematically studied. They were divided into 10 groups on the basis of their phenotypic characteristics and 16S rRNA gene sequence analyses. The Gram-positive coccal isolates in Group I (3 isolates), Group II (3 isolates) and Group III (1 isolate) showed 99.2%, 99.5-99.7% and 99.8% sequences similarity to Staphylococcus saprophyticus, S. napalensis and S. sciuri, respectively. Each Gram-positive rod-shaped isolates in Group IV and V belonged to the genus Bacillus and was closely related to B. vietnamensis and B. safensis with 99.2% and 99.4% sequences similarity, respectively. The Gram-positive, moderately halophilic rod-shaped bacteria in Group VI (3 isolates), Group VII (1 isolate), Group VIII (1 isolate) and Group IX (2 isolates) were closely related to Virgibacillus halodenitrificans (98.5-99.1%), Oceanobacillus iheyensis (99.3%), Halobacillus mangrove (97.9%) and H. dabanensis (98.5-98.6%), respectively. One Gram-negative isolate of moderately halophilic bacterium (Group X) was closely related to Idiomarina zobelli (98.0%). They possessed phosphatase activities ranged from 10.08-70.96 U ml-1 . The isolate NSW 13-2 (Group VI) showed the highest ALP.

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“…41 Obviously, the reason is that the equilibrium concentration of zinc ions in inorganic buffer solutions is higher than in organic ones whose components can form stable complexes with zinc. When zinc concentration is > 5 µg mL -1 , the degree of phosphatase inhibition does not change in any of the buffer solutions, apparently, because of saturation of the zinc binding enzyme sites by metal ions at high contents of the metal in the reaction mixture.…”

Section: Increase In the Sensitivity Of Determination Of In Hibitorsmentioning

confidence: 99%

“…When zinc concentration is > 5 µg mL -1 , the degree of phosphatase inhibition does not change in any of the buffer solutions, apparently, because of saturation of the zinc binding enzyme sites by metal ions at high contents of the metal in the reaction mixture. 41 The concentration of the buffer solution is equally important in determining the degree of inhibition of alka line phosphatase by metal ions. For example, in the case of alkaline phosphatase from E. coli, the concentration of metal ions required to attain the same inhibition degree increases by two orders of magnitude on going from 0.05 to 0.1 M Tris HCl buffer solution.…”

Section: Increase In the Sensitivity Of Determination Of In Hibitorsmentioning

confidence: 99%

Enzymatic methods of analysis: Novel approaches and applications

2007

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The results of a series of investigations dealing with the development of enzymatic methods for determination of biologically active compounds, viz., inhibitors, activators, and substrates of native and immobilized enzymes of the oxidoreductase (peroxidases, alcohol dehydro genases) and hydrolase (alkaline and acid phosphatases) classes isolated from diverse sources are summarized. Novel original approaches, proposed by the authors, for improving the sensi tivity, selectivity, and rapidity of the methods are discussed. Numerous examples of application of the developed enzymatic procedures for the analysis of a wide range of samples are given.

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Application of Alkaline Phosphatases from Different Sources in Pharmaceutical and Clinical Analysis for the Determination of Their Cofactors; Zinc and Magnesium Ions

Cited by 22 publications

References 23 publications

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Stability Improvement of Immobilized Alkaline Phosphatase Using Chitosan Nanoparticles

Characterization of Alkaline Phosphatase Producing Bacteria Isolated from Thai Fermented Fish Products

Enzymatic methods of analysis: Novel approaches and applications

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