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

Xie, Xiao-Lan; Du, Juan; Huang, Qiang-Sheng; Shi, Yan; Chen, Qing‐Xi

doi:10.1016/j.ijbiomac.2007.03.010

Cited by 9 publications

(9 citation statements)

References 23 publications

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“…At each concentration of citric acid, the reaction rate decreased with increasing time until a straight line was approached, the slope of which decreased with increasing citric acid concentration. The above results as analyzed by Tsou's method [16] suggested that the formation of the enzyme-inhibitor (citric acid) complex was a slow, reversible reaction (curves 1e5 in Fig. 4a).…”

Section: Kinetics Of the Substrate Reaction In The Presence Of Differmentioning

confidence: 82%

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

Xie

Wang

et al. 2010

Fish & Shellfish Immunology

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Section: Kinetics Of the Substrate Reaction In The Presence Of Differmentioning

confidence: 82%

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

Xie

Wang

et al. 2010

Fish & Shellfish Immunology

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“…For slow, reversible, and noncompetitive inhibition with fractional residue activity, the kinetic model of the enzyme reacting with the substrate and the inhibitor can be written as (16) …”

Section: Methodsmentioning

confidence: 99%

“…In our previous investigations, we found that Hg 2+ could influence the conformation and activity of L. vannamei NAGase and only one molecule of HgCl 2 binding with the enzyme molecule could make irreversible inactivation of prawn NAGase (13). The histidine or cysteine residues are essential residues to prawn NAGase activity (13, 16). Therefore, we presumed that Zn 2+ induced the changes of prawn NAGase activity and conformation by binding with the histidine or cysteine residues.…”

Section: Dicussionmentioning

confidence: 99%

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Inhibitory kinetics of β‐N‐acetyl‐D‐glucosaminidase from prawn (Litopenaeus vannamei) by zinc ion

et al. 2008

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SummaryPrawn (Litopenaeus vannamei) b-N-acetyl-D-glucosaminidase (NAGase, EC 3.2.1.52) is involved in the digestion and molting processes. Zinc is one of the most important metals often found in the pollutant. In this article, the effects of Zn 2þ on prawn NAGase activity for the hydrolysis of pNP-NAG have been investigated. The results showed that Zn 2þ could reversibly and noncompetitively inhibit the enzyme activity at appropriate concentrations and its IC 50 value was estimated to be 6.00 6 0.25 mM. The inhibition model was set up, and the inhibition kinetics of the enzyme by Zn 2þ has been studied using the kinetic method of the substrate reaction. The inhibition constant was determined to be 11.96 mM and the microscopic rate constants were also determined for inactivation and reactivation. The rate constant of the inactivation (k þ0 ) is much larger than that of the reactivation (k 20 ). Therefore, when the Zn 2þ concentration is sufficiently large, the enzyme is completely inactivated. On increasing the concentration of Zn 2þ , the fluorescence emission peak and the UV absorbance peak are not position shifted, but the intensity decreased, indicating that the conformation of Zn 2þ -bound inactive NAGase is stable and different from that of native NAGase. We presumed that Zn 2þ made changes in the activity and conformation of prawn NAGase by binding with the histidine or cysteine residues of the enzyme.

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“…Indeed, most articles listed in Table 3 [103,104,105,106,107,108,109,110,111,112,113,114,115,116,117,118,119,120,121,122,123,124,125,126,127,128,129,130,131,132,133,134] focused on bioprocesses for the synthesis of useful products and on enzymatic routes adopted for setting up laboratory techniques to study marine complex biomolecules (e.g., improving extraction, digestion of polysaccharides to simple components for structural determination, etc.). Various examples are found in the literature of the synthesis and hydrolysis of glycosidic bonds.…”

Section: Fine Chemistry and Lab Techniquesmentioning

confidence: 99%

Enzymatic Processes in Marine Biotechnology

Trincone

2017

Marine Drugs

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In previous review articles the attention of the biocatalytically oriented scientific community towards the marine environment as a source of biocatalysts focused on the habitat-related properties of marine enzymes. Updates have already appeared in the literature, including marine examples of oxidoreductases, hydrolases, transferases, isomerases, ligases, and lyases ready for food and pharmaceutical applications. Here a new approach for searching the literature and presenting a more refined analysis is adopted with respect to previous surveys, centering the attention on the enzymatic process rather than on a single novel activity. Fields of applications are easily individuated: (i) the biorefinery value-chain, where the provision of biomass is one of the most important aspects, with aquaculture as the prominent sector; (ii) the food industry, where the interest in the marine domain is similarly developed to deal with the enzymatic procedures adopted in food manipulation; (iii) the selective and easy extraction/modification of structurally complex marine molecules, where enzymatic treatments are a recognized tool to improve efficiency and selectivity; and (iv) marine biomarkers and derived applications (bioremediation) in pollution monitoring are also included in that these studies could be of high significance for the appreciation of marine bioprocesses.

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

Cited by 9 publications

References 23 publications

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

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

Inhibitory kinetics of β‐N‐acetyl‐D‐glucosaminidase from prawn (Litopenaeus vannamei) by zinc ion

Enzymatic Processes in Marine Biotechnology

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