Enzymatic hydrolysis of bis-(4-nitrophenyl)phosphate and bis-(4-cyanophenyl)phosphate by rat tissues

1978 ◽  
Vol 27 (5) ◽  
pp. 733-737 ◽  
Author(s):  
Ernst Brandt ◽  
Eberhard Heymann
Keyword(s):  
Enzymatic Hydrolysis ◽  
Rat Tissues ◽  
Nitrophenyl Phosphate ◽  
Hydrolysis Of

scholarly journals Subcellular localization and tissue distribution of sialic acid-forming enzymes. N-acetylneuraminate-9-phosphate synthase and N-acetylneuraminate 9-phosphatase

1984 ◽  
Vol 223 (2) ◽  
pp. 323-328 ◽  
Author(s):  
J Van Rinsum ◽  
W Van Dijk ◽  
G J Hooghwinkel ◽  
W Ferwerda
Keyword(s):  
Subcellular Localization ◽  
Biosynthetic Pathway ◽  
Cytosolic Fraction ◽  
Phosphate Esters ◽  
Rat Tissues ◽  
Acetylneuraminic Acid ◽  
Nitrophenyl Phosphate ◽  
Sucrose Medium ◽  
Hydrolysis Of ◽  
Phosphate Synthase

The activities of N-acetylneuraminate 9-phosphate synthase and N-acetylneuraminate 9-phosphatase, the two enzymes involved in the final steps of the biosynthetic pathway of N-acetylneuraminic acid, were measured with the substrates N-acetyl[14C]mannosamine 6-phosphate and N-acetyl[14C]neuraminic acid 9-phosphate respectively. Subcellular localization studies in rat liver indicated that both enzymes are localized in the cytosolic fraction after homogenization in sucrose medium. To test the possibility of misinterpretation due to the hydrolysis of N-acetylneuraminic acid 9-phosphate by non-specific phosphatases, the hydrolysis of various phosphate esters by the cytosolic fraction was tested. Only p-nitrophenyl phosphate was hydrolysed; however, competition studies with N-acetylneuraminic acid 9-phosphate and p-nitrophenyl phosphate indicated that two different enzymes were involved and that no competition existed between the two substrates. In various other rat tissues N-acetylneuraminate-9-phosphate synthase and N-acetylneuraminate 9-phosphatase activities were detected, suggesting that N-acetylmannosamine 6-phosphate is a general precursor for N-acetylneuraminic acid biosynthesis in all the tissues studied.

THE NON-ENZYMATIC HYDROLYSIS OF p-NITROPHENYL PHOSPHATE

1958 ◽  
Vol 36 (4) ◽  
pp. 686-690 ◽  
Author(s):  
K. A. Holbrook ◽  
Ludovic Ouellet
Keyword(s):  
Activation Energy ◽  
Enzymatic Hydrolysis ◽  
Ionic Species ◽  
Kcal Mole ◽  
First Order ◽  
Colorimetric Measurement ◽  
Nitrophenyl Phosphate ◽  
Ph Range ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of the non-enzymatic hydrolysis of p-nitrophenyl phosphate have been studied in aqueous solution in the pH range 2.6 to 9.0 and at temperatures from 68.0°to 82.0 °C. The reaction has been followed by colorimetric measurement of the nitrophenol produced by the reaction[Formula: see text]The reaction is first order with respect to p-nitrophenyl phosphate and has an activation energy of 26.0 kcal./mole at pH 2.6. An explanation has been proposed in terms of the different rates of hydrolysis of the various ionic species of the ester present in solution.

THE WHEAT LEAF PHOSPHATASES: VII. FURTHER STUDIES ON INHIBITORS AT pH 5.7

1963 ◽  
Vol 41 (1) ◽  
pp. 1727-1731 ◽  
Author(s):  
D. W. A. Roberts
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Hydrolysis ◽  
Inhibitory Effect ◽  
Substrate Specificities ◽  
Nitrophenyl Phosphate ◽  
Wheat Leaf ◽  
Hydrolysis Of

A survey of the inhibitory effect of various ribonucleosides, deoxyribonucleosides, sugars, phenols, and vitamins on the hydrolysis of 17 phosphatase substrates has been made. The more soluble ribonucleosides and deoxyribonucleosides inhibited the enzymatic hydrolysis of adenosine 5′-phosphate, phenolphthalein diphosphate, phenylphosphate, p-nitrophenyl phosphate, and in some cases the hydrolysis of adenosine 3′-phosphate, adenosine 2′-phosphate, and riboflavin 5′-phosphate. A 0.02 M concentration of orthophosphate inhibited the hydrolysis of all the compounds tested except adenosine 5′-phosphate and phenolphthalein diphosphate.These results, together with earlier findings, are discussed in terms of the concept that wheat leaf press juice contains two types of acid phosphatase, namely, β-glycerophosphatase and adenosine 5′-phosphatase. These two types of enzyme appear to have partially overlapping substrate specificities.

THE WHEAT LEAF PHOSPHATASES: VII. FURTHER STUDIES ON INHIBITORS AT pH 5.7

1963 ◽  
Vol 41 (8) ◽  
pp. 1727-1731 ◽  
Author(s):  
D. W. A. Roberts
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Hydrolysis ◽  
Inhibitory Effect ◽  
Substrate Specificities ◽  
Nitrophenyl Phosphate ◽  
Wheat Leaf ◽  
Hydrolysis Of

A survey of the inhibitory effect of various ribonucleosides, deoxyribonucleosides, sugars, phenols, and vitamins on the hydrolysis of 17 phosphatase substrates has been made. The more soluble ribonucleosides and deoxyribonucleosides inhibited the enzymatic hydrolysis of adenosine 5′-phosphate, phenolphthalein diphosphate, phenylphosphate, p-nitrophenyl phosphate, and in some cases the hydrolysis of adenosine 3′-phosphate, adenosine 2′-phosphate, and riboflavin 5′-phosphate. A 0.02 M concentration of orthophosphate inhibited the hydrolysis of all the compounds tested except adenosine 5′-phosphate and phenolphthalein diphosphate.These results, together with earlier findings, are discussed in terms of the concept that wheat leaf press juice contains two types of acid phosphatase, namely, β-glycerophosphatase and adenosine 5′-phosphatase. These two types of enzyme appear to have partially overlapping substrate specificities.

Sex differences in the enzymatic hydrolysis of acetylsalicylic acid by microsomes from various rat tissues

1997 ◽  
Vol 17 (6) ◽  
pp. 347-351 ◽  
Author(s):  
Ana Ma. Julieta Vargas Loza ◽  
Elsa I. Sánchez Montes De Oca ◽  
Francisco A. Posadas Del Rio
Keyword(s):  
Sex Differences ◽  
Enzymatic Hydrolysis ◽  
Acetylsalicylic Acid ◽  
Rat Tissues ◽  
Hydrolysis Of

Enzymatic hydrolysis of isocarboxazid by rat tissues

1971 ◽  
Vol 20 (2) ◽  
pp. 504-507 ◽  
Author(s):  
Satoh Tetsuo ◽  
Moroi Kayoko
Keyword(s):  
Enzymatic Hydrolysis ◽  
Rat Tissues ◽  
Hydrolysis Of

Microwave-assisted enzymatic hydrolysis of starch

2009 ◽  
Author(s):  
Marcin Lukasiewicz ◽  
Anna Osowiec ◽  
Magdalena Marciniak
Keyword(s):  
Enzymatic Hydrolysis ◽  
Microwave Assisted ◽  
Hydrolysis Of

Analyses of enzymatic hydrolysis of bagasse cane of sugar for obtention of ethanol employing a cocktail of natives commercials enzymes.  

2018 ◽  
Author(s):  
Ángel Batallas ◽  
Erenio González ◽  
Carmen Salvador ◽  
Jonathan Villavicencio ◽  
Humberto González Gavilánez ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Hydrolysis Of

Immobilized Nanoparticles-Mediated Enzymatic Hydrolysis of Cellulose for Clean Sugar Production: A Novel Approach

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai
Keyword(s):  
Catalytic Activity ◽  
Enzymatic Hydrolysis ◽  
Immobilized Enzyme ◽  
Free Enzyme ◽  
Magnetic Nanomaterials ◽  
Sugar Production ◽  
Cellulase Enzyme ◽  
Enzymatic Hydrolysis Of Cellulose ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.

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