Formation of Protein–Birnessite Complex: XRD, FTIR, and AFM Analysis

Naidja, A.; Liu, C.; Huang, P. M.

doi:10.1006/jcis.2002.8349

Cited by 65 publications

(34 citation statements)

References 46 publications

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“…Protein disintegration after contact with birnessite surfaces was recently corroborated by Reardon et al (2016) and the mechanism of fragmentation identified as hydrolysis. The reports of Russo et al (2009) and Reardon et al (2016) are in contrast to the work of Naidja et al (2002), who identified birnessite as a strong adsorbent for protein. If we assume both types of observations to be valid, i.e.…”

Section: Introductioncontrasting

confidence: 72%

Differential capacity of kaolinite and birnessite to protect surface associated proteins against thermal degradation

Chacon

García-Jaramillo

Liu

et al. 2018

Soil Biology and Biochemistry

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Soil organic carbon cycling depends on the presence and catalytic functionality of extracellular proteins. The mineral matrix has the capacity to enhance, maintain or impede this functionality through a variety of mechanisms. The goal of this research was to identify some of the mechanisms involved in determining the role of the mineral matrix towards proteins. To this end, we adsorbed Beta-Glucosidase (BG) and Bovine Serum Albumin (BSA) on the phyllosilicate kaolinite and the manganese oxide acid birnessite at pH 5 and pH 7. The protein-mineral samples were then subjected to gradual energy inputs equivalent to an intense forest fire using a laser and the abundance and molecular masses of desorbed organic compounds were recorded after ionization with tunable synchrotron ultravacuum vacuum ultraviolet radiation (VUV). We found that the mechanisms controlling the fate of proteins varied with mineralogy. Kaolinite adsorbed protein largely through hydrophobic interactions and produced negligible amounts of desorption fragments compared to birnessite, even at energy inputs equivalent to an intense forest fire. Acid birnessite adsorbed protein through coulombic forces at low energy levels, became a hydrolyzing catalyst at low energies and low pH and eventually turned into a reactant involving disintegration of both mineral and protein at higher energy inputs. Fragmentation of proteins was energy dependent, and did not occur below an energy threshold of 0.20 MW cm -2 . Neither signal abundance nor signal intensity were a function of protein size. Above the energy threshold value, BG adsorbed to birnessite at pH 7 showed an increase in signal abundance with increasing energy applications.. Signal intensities differed with adsorption pH for BSA but only at the highest energy level applied. Our results indicate that proteins adsorbed to kaolinite are likely to remain intact

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Section: Introductioncontrasting

confidence: 72%

Differential capacity of kaolinite and birnessite to protect surface associated proteins against thermal degradation

Chacon

García-Jaramillo

Liu

et al. 2018

Soil Biology and Biochemistry

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“…These changes indicate that the adsorption on the silica matrix successfully took place [34] and one can draw some conclusions on the secondary structure of the peptide after the immobilization [35,36]. The presence of amide I and amide II bands may also be proof that the immobilized enzyme could have preserved its activity [36].…”

Section: Evaluation Of the Hydrolytic Activity Ofmentioning

confidence: 88%

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Zdarta

Sałek

Kołodziejczak-Radzimska

et al. 2014

Open Chemistry

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The immobilization of Amano Lipase A fromAspergillus niger by adsorption onto Stöber silica matrix obtained by sol-gel method was studied. The effectiveness of the enzyme immobilization and thus the usefulness of the method was demonstrated by a number of physicochemical analysis techniques including Fourier Transform Infrared Spectroscopy (FT-IR), elemental analysis (EA), thermogravimetric analysis (TG), porous structure of the support and the products after immobilization from the enzyme solution with various concentration at different times. The analysis of the process' kinetics allowed the determination of the sorption parameters of the support and optimization of the process. The optimum initial concentration of the enzyme solution was found to be 5 mg mL -1 , while the optimum time of the immobilization was 120 minutes. These values of the variable parameters of the process were obtained by as ensuring the immobilization of the largest possible amount of the biocatalyst at the most economically beneficial aspects of the process.

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“…The data presented here suggest that MnO 2 can degrade PrP TSE in soil environments. Previous studies reported loss of protein from solution when incubated with MnO 2 and ascribed the losses to sorption to MnO 2 surfaces (Naidja et al, 2002;Rao et al, 2007). Treatment of BH with d-MnO 2 (Fig.…”

mentioning

confidence: 99%

Pathogenic prion protein is degraded by a manganese oxide mineral found in soils

Russo

Johnson

McKenzie

et al. 2009

Journal of General Virology

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Formation of Protein–Birnessite Complex: XRD, FTIR, and AFM Analysis

Cited by 65 publications

References 46 publications

Differential capacity of kaolinite and birnessite to protect surface associated proteins against thermal degradation

Differential capacity of kaolinite and birnessite to protect surface associated proteins against thermal degradation

Immobilization of Amano Lipase A onto Stöber silica surface: process characterization and kinetic studies

Pathogenic prion protein is degraded by a manganese oxide mineral found in soils

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