Purification and Characterization of a &amp;#946;-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.

Pereira, Wogelsanger Oliveira; Cruz, Ana Katarina Menezes da; Albuquerque, Elizabeth M.M.; Santos, Elizeu A.; Oliveira, Adeliana S.; Sales, Maurı́cio P.; Oliveira, Fernanda W.

doi:10.2174/0929866054696055

Cited by 5 publications

(2 citation statements)

References 16 publications

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“…GLH (43 kDa), Scutellaria root (55–58 kDa) and Pomacea sp . (90 kDa) . These differences could be engendered by genetic variations present among different species, which play important roles in determining the size, shape and molecular mass of such enzymes.…”

Section: Discussionmentioning

confidence: 99%

Purification, characterization and comparison of Penicillium purpurogenum β‐glucuronidases expressed in Escherichia coli and Pichia pastoris

Zou

Guo

Kaleem

et al. 2013

J of Chemical Tech & Biotech

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Background To investigate the effects of post‐translational modifications in different recombinant expression systems on the catalytic properties of recombinant β‐glucuronidase. The β‐glucuronidase (GUS) gene from Penicillium purpurogenum Li‐3 was cloned and successfully expressed in Escherichia coli BL21 and Pichia pastoris G115. Results The recombinant E. coli produced a 15‐fold increased level of β‐glucuronidase while the recombinant P. pastoris strain produced a 6.9‐fold increased level of β‐glucuronidase compared with their parent strains. The β‐glucuronidases from recombinant E. coli (PGUS‐E) and P. pastors (PGUS‐P) were purified to 35.9‐ and 47.4‐fold, respectively, through affinity, ion exchange and gel filtration chromatography. PGUS‐E from E. coli was a non‐glycosylated protein with an apparent molecular mass of 72.43 kDa, while PGUS‐P from P. pastors was appropriately glycosylated with a molecular mass of 78.83 kDa measured by MALDI/TOF‐MS. Although both recombinant β‐glucuronidases exhibited similar pH optima, the glycosylated PGUS‐P showed a significantly higher thermal stability and less sensitivity to metal ions compared with the non‐glycosylated PGUS‐E. The glycosylated PGUS‐P also displayed lower Km values, and higher kcat/Km ratios than the non‐glycosylated enzyme towards glycyrrhizin. Conclusion These results revealed the key role of post‐translational modifications in the P. pastors expression system on the catalytic properties of β‐glucuronidase and its potential stability over the prokaryotic expression system which could be applied as an important tool for the functional enhancement of industrial enzymes. © 2013 Society of Chemical Industry

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Section: Discussionmentioning

confidence: 99%

Purification, characterization and comparison of Penicillium purpurogenum β‐glucuronidases expressed in Escherichia coli and Pichia pastoris

Zou

Guo

Kaleem

et al. 2013

J of Chemical Tech & Biotech

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“…Acute renal necrosis, cancer of urinary bladder, and active pyelonephritis are some urinary disorders and causes due to increasing the level of this enzyme (3). The glycoside hydrolases family can be isolated from many organisms including humans (4), animals (5,6), plants (7), and bacteria (8).…”

Section: Introductionmentioning

confidence: 99%

Design of Novel Benzimidazole Derivatives as Potential α-amylase Inhibitors by 3D-QSAR Modeling and Molecular Docking Studies

Khatabi

Aanouz

El-Mernissi

et al. 2020

Journal of the Turkish Chemical Society Section A: Chemistry

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The enzyme α-amylase belongs to the highly conserved glycoside hydrolase family which is regarded as a good target for the discovery of antidiabetic agents. Following a 3D-QSAR study on forty-five 2-aryl benzimidazole derivatives which have been reported as potential insulin-independent antidiabetic agents. The results revealed that the CoMFA values were found to be 0.696 and 0.860 for Q 2 and R 2 respectively; while for the CoMSIA, the Q 2 and R 2 values were found to be 0.514 and 0.852 respectively. Both models were derived from a training set of thirty-seven compounds based on an appropriate method of alignment, while the predictive ability was approved by a test set containing eight compounds with r ext 2 values of 0.990 and 0.987, respectively. Moreover, the contour maps generated from CoMFA and CoMSIA models provided much helpful information to figure out the structural requirements that influence the activity. To further reinforce the 3D-QSAR results, the molecular docking method was implemented which led to the design of new potential insulin-independent antidiabetic compounds with high predicted activity values.

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Synthesis and biological evaluation of novel N-arylidenequinoline-3-carbohydrazides as potent β-glucuronidase inhibitors

Taha

Sultan

Nuzar

et al. 2016

Bioorganic & Medicinal Chemistry

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Purification and Characterization of a β-Glucuronidase Present During Embryogenesis of the Mollusk Pomacea sp.

Cited by 5 publications

References 16 publications

Purification, characterization and comparison of Penicillium purpurogenum β‐glucuronidases expressed in Escherichia coli and Pichia pastoris

Purification, characterization and comparison of Penicillium purpurogenum β‐glucuronidases expressed in Escherichia coli and Pichia pastoris

Design of Novel Benzimidazole Derivatives as Potential α-amylase Inhibitors by 3D-QSAR Modeling and Molecular Docking Studies

Synthesis and biological evaluation of novel N-arylidenequinoline-3-carbohydrazides as potent β-glucuronidase inhibitors

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