Inhibitory kinetics of citric acid on β-N-acetyl-d-glucosaminidase from prawn (Litopenaeus vannamei)

Xie, Xiao-Lan; Hu, Yonghua; Wang, Lingling; Chen, Chaoqi; Huang, Qingjiu; Zhou, Hantao; Chen, Qing‐Xi

doi:10.1016/j.fsi.2010.07.004

Cited by 8 publications

(3 citation statements)

References 32 publications

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“…The results showed that the inhibition was a reversible reaction with fractional residual enzyme activity. This can be written as shown in Scheme 1 (11), where E, S, I, and P denote enzyme, substrate, inhibitor (zinc), and product, respectively. EI, ES, and EIS are the respective compounds.…”

Section: Methodsmentioning

confidence: 99%

Inhibitory Kinetics of β-N-Acetyl-d-glucosaminidase from Green Crab (Scylla serrata) by Zinc Ion

Zhang

Wang

et al. 2010

J. Agric. Food Chem.

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Heavy metal pollution such as chromium and zinc in the seawater has been increasing in recent years in the China Sea. Marine shellfish such as prawn and crab are sensitive to this pollution. Beta-N-acetyl-d-glucosaminidase (NAGase, EC 3.2.1.52) catalyzes the cleavage the oligomers of N-acetylglucosamine (NAG) into the monomer. In this study, taking p-nitrophenyl-N-acetyl-beta-d-glucosaminide (pNP-NAG) as substrate, the effects of Zn(2+) on NAGase from green crab ( Scylla serrata ) have been studied. The results showed that appropriate concentrations of zinc could lead to reversible inhibition on the enzyme, and the IC(50) has been estimated to be 0.5 +/- 0.012 mM. Furthermore, it has been shown that Zn(2+) could reduce the thermal stability of NAGase depending on the concentration of Zn(2+). The inhibitory kinetics of zinc on the enzyme in the appropriate concentrations has been studied using the kinetic method of substrate reaction. The inhibition model has been set up, and the rate constants have been determined. The results showed that Zn(2+) was a mixed-type inhibitor of NAGase and that it could combine at the free enzyme and the enzyme-substrate active sites.

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Section: Methodsmentioning

confidence: 99%

Inhibitory Kinetics of β-N-Acetyl-d-glucosaminidase from Green Crab (Scylla serrata) by Zinc Ion

Zhang

Wang

et al. 2010

J. Agric. Food Chem.

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“…However, the in vitro approach of NAGase alteration has been poorly investigated because the sampled crustaceans were weakly diversified (i.e., NAGase extracted from the Brachyura, S. serrata , or the Penaeide, L. vannamei ). Notwithstanding, these investigations revealed a direct alteration of NAGase by heavy metals (Lin, Wang et al, 2005; Lin, Xie et al, 2006; Yang et al, 2006; Zhang et al, 2010), antibiotics (Du et al, 2008; Yan et al, 2007), organic disinfectant agents (Lin et al, 2005; Xie et al, 2009), and amino acids (Xie et al., 2006). The sensitivity of NAGase activity has never been studied in caridean shrimps, which include several species of economical and ecological interests.…”

Section: Introductionmentioning

confidence: 99%

Effects of Chemical Compounds on the Activity of the N‐acetyl‐β‐D‐Glucosaminidase of the Marine Prawn, Palaemon serratus: Screening In Vitro

Rollin

Coulaud

Rocher

et al. 2023

Enviro Toxic and Chemistry

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N‐acetyl‐β‐D‐glucosaminidase (NAGase) is important for crustaceans because the enzyme activity is necessary for the molting process. The present study aimed to assess the sensitivity of Palaemon serratus NAGase activity to a set of compounds of diverse chemical families in the context of in vitro exposures. Compounds representing different chemical families were selected according to their abundance, impact in the environment, and relevance as disruptors of the molting process. In a first step, four solvents (dimethylsulfoxide [DMSO], methanol, acetone, and ethanol) were tested to determine their suitability to dissolve hydrophobic compounds without affecting NAGase activity. Exclusively, ethanol had no effect on enzyme activity and on the integrity of the proteins present in the enzyme extract. The 18 other compounds were tested and four of these compounds, pentoxifylline, fenoxycarb, dithiocarbamate, and RH5849, showed a specific alteration on the activity of NAGase, without affecting the protein content. However, cadmium, zinc, and glyphosate showed a nonspecific alteration, affecting both the enzyme activity and the proteins, whereas ibuprofen exclusively altered the protein content. Finally, 10 of the 22 tested compounds (including DMSO, acetone, and methanol) showed a direct alteration of NAGase activity. Environ Toxicol Chem 2023;42:846–858. © 2023 SETAC

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“…Prawn ( Litopenaeus vannamei ) is one of the most popular farmed prawns in the world. At present, systematical studies of NAGase from L. vannamei are taking place in our laboratory − .…”

Section: Introductionmentioning

confidence: 99%

Inhibitory Kinetics of Betaine on β-N-Acetyl-d-glucosaminidase from Prawn (Litopenaeus vannamei)

Xie

Zhou

Huang

et al. 2010

J. Agric. Food Chem.

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The effects of betaine on prawn beta-N-acetyl-D-glucosaminidase (NAGase) activity for the hydrolysis of p-nitrophenyl-N-acetyl- beta-D-glucosaminide (pNP-NAG) have been studied. The results showed that appropriate concentrations of betaine could lead to reversible inhibition against NAGase, and the IC(50) value was estimated to be 15.00 +/- 0.30 mM. The inhibitory kinetics assay showed that betaine was a mixed type inhibitor with a K(I) value of 9.17 +/- 0.85 mM and a K(IS) value of 45.58 +/- 2.52 mM. The inhibitory model was set, and the microscopic rate constants were determined using the kinetic method of the substrate reaction. The time course of the hydrolysis of pNP-NAG catalyzed by NAGase in the presence of different betaine concentrations showed that at each betaine concentration, the rate decreased with an increase in time until a straight line was approached, indicating that the inhibition of NAGase by betaine is a slow, reversible reaction with fractional residual activity. The fact that k(+0) is much larger than k(+0)(') indicated that the free enzyme molecule is more fragile than the enzyme-substrate complex against betaine. It is suggested that the presence of the substrate offers marked protection of NAGase against inhibition by betaine.

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Inhibitory kinetics of citric acid on β-N-acetyl-d-glucosaminidase from prawn (Litopenaeus vannamei)

Cited by 8 publications

References 32 publications

Inhibitory Kinetics of β-N-Acetyl-d-glucosaminidase from Green Crab (Scylla serrata) by Zinc Ion

Inhibitory Kinetics of β-N-Acetyl-d-glucosaminidase from Green Crab (Scylla serrata) by Zinc Ion

Effects of Chemical Compounds on the Activity of the N‐acetyl‐β‐D‐Glucosaminidase of the Marine Prawn, Palaemon serratus: Screening In Vitro

Inhibitory Kinetics of Betaine on β-N-Acetyl-d-glucosaminidase from Prawn (Litopenaeus vannamei)

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