Adsorption of ethylenediaminetetraacetic dianhydride modified oxalate decarboxylase on calcium oxalate. (3rd April 2018)
- Record Type:
- Journal Article
- Title:
- Adsorption of ethylenediaminetetraacetic dianhydride modified oxalate decarboxylase on calcium oxalate. (3rd April 2018)
- Main Title:
- Adsorption of ethylenediaminetetraacetic dianhydride modified oxalate decarboxylase on calcium oxalate
- Authors:
- Cai, XH
Lin, RH
Wu, J
He, JB
Wu, YC
Wang, XY - Abstract:
- Abstract: We used ethylenediaminetetraacetic acid dianhydride (EDTAD) to modify oxalate decarboxylase (OXDC) to improve its adsorption on calcium oxalate stones. The modified sites were identified by Ultra performance liquid chromatography-mass spectrometry (UPLC-MS) and the adsorption mechanism of the EDTAD-modified OXDC on calcium oxalate (CaOx) was investigated. We investigated adsorption time, initial enzyme concentration, temperature and solution pH on the adsorption process. Data were analyzed using kinetics, thermodynamics and isotherm adsorption models. UPLC-MS showed that EDTAD was attached to OXDC covalently and suggested that the chemical modification occurred at both the free amino of the side chain and the α-NH2 of the peptide. The adsorption capacity of the EDTAD-OXDC on calcium oxalate was 53.37% greater than that of OXDC at the initial enzyme concentration of 5 mg/ml, pH = 7.0, at 37° C. The modified enzyme (EDTAD-OXDC) demonstrated improved oxalate degradation activity at pH 4.5−6.0. Kinetic data fitting analysis suggested a pseudo second order kinetic model. Estimates of the thermodynamic parameters including ΔG 0, ΔH 0 and ΔS 0 of the adsorption process showed it to be feasible, spontaneous and endothermic. Isotherm data fitting analysis indicated that the adsorption process is reduced to monolayer adsorption at a low enzyme concentration and to multilayer adsorption at a high enzyme concentration. It may be possible to apply OXDC to degradation ofAbstract: We used ethylenediaminetetraacetic acid dianhydride (EDTAD) to modify oxalate decarboxylase (OXDC) to improve its adsorption on calcium oxalate stones. The modified sites were identified by Ultra performance liquid chromatography-mass spectrometry (UPLC-MS) and the adsorption mechanism of the EDTAD-modified OXDC on calcium oxalate (CaOx) was investigated. We investigated adsorption time, initial enzyme concentration, temperature and solution pH on the adsorption process. Data were analyzed using kinetics, thermodynamics and isotherm adsorption models. UPLC-MS showed that EDTAD was attached to OXDC covalently and suggested that the chemical modification occurred at both the free amino of the side chain and the α-NH2 of the peptide. The adsorption capacity of the EDTAD-OXDC on calcium oxalate was 53.37% greater than that of OXDC at the initial enzyme concentration of 5 mg/ml, pH = 7.0, at 37° C. The modified enzyme (EDTAD-OXDC) demonstrated improved oxalate degradation activity at pH 4.5−6.0. Kinetic data fitting analysis suggested a pseudo second order kinetic model. Estimates of the thermodynamic parameters including ΔG 0, ΔH 0 and ΔS 0 of the adsorption process showed it to be feasible, spontaneous and endothermic. Isotherm data fitting analysis indicated that the adsorption process is reduced to monolayer adsorption at a low enzyme concentration and to multilayer adsorption at a high enzyme concentration. It may be possible to apply OXDC to degradation of calcium oxalate stones. … (more)
- Is Part Of:
- Biotechnic & histochemistry. Volume 93:Number 3(2018)
- Journal:
- Biotechnic & histochemistry
- Issue:
- Volume 93:Number 3(2018)
- Issue Display:
- Volume 93, Issue 3 (2018)
- Year:
- 2018
- Volume:
- 93
- Issue:
- 3
- Issue Sort Value:
- 2018-0093-0003-0000
- Page Start:
- 220
- Page End:
- 229
- Publication Date:
- 2018-04-03
- Subjects:
- adsorption -- calcium oxalate -- ethylenediaminetetraacetic acid dianhydride -- oxalate decarboxylase
Histochemistry -- Periodicals
Stains and staining (Microscopy) -- Periodicals
Biotechnology -- Periodicals
572 - Journal URLs:
- http://informahealthcare.com/loi/bih ↗
http://www.bios.co.uk/journals/bh/index.htm ↗
http://informahealthcare.com ↗ - DOI:
- 10.1080/10520295.2017.1420820 ↗
- Languages:
- English
- ISSNs:
- 1052-0295
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2089.777000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 6759.xml