LIVIVO - Search results -

Search results

Result 1 - 10 of total 44

Search options

Article ; Online: Structural Transitions of Papain-like Cysteine Proteases: Implications for Sensor Development.

Marković, Srdjan / Andrejević, Natalija S / Milošević, Jelica / Polović, Natalija Đ

Biomimetics (Basel, Switzerland)

2023 Volume 8, Issue 3

Abstract: The significant role of papain-like cysteine proteases, including papain, cathepsin L and SARS-CoV-2 PLpro, in biomedicine and biotechnology makes them interesting model systems for sensor development. These enzymes have a free thiol group that is ... ...

Abstract	The significant role of papain-like cysteine proteases, including papain, cathepsin L and SARS-CoV-2 PLpro, in biomedicine and biotechnology makes them interesting model systems for sensor development. These enzymes have a free thiol group that is suitable for many sensor designs including strong binding to gold nanoparticles or low-molecular-weight inhibitors. Focusing on the importance of the preservation of native protein structure for inhibitor-binding and molecular-imprinting, which has been applied in some efficient examples of sensor development, the aim of this work was to examine the effects of the free-thiol-group's reversible blocking on papain denaturation that is the basis of its activity loss and aggregation. To utilize biophysical methods common in protein structural transitions characterization, such as fluorimetry and high-resolution infrared spectroscopy, low-molecular-weight electrophilic thiol blocking reagent S-Methyl methanethiosulfonate (MMTS) was used in solution. MMTS binding led to a two-fold increase in 8-Anilinonaphthalene-1-sulfonic acid fluorescence, indicating increased hydrophobic residue exposure. A more in-depth analysis showed significant transitions on the secondary structure level upon MMTS binding, mostly characterized by the lowered content of α-helices and unordered structures (either for approximately one third), and the increase in aggregation-specific β-sheets (from 25 to 52%) in a dose-dependant manner. The recovery of this inhibited protein showed that reversibility of inhibition is accompanied by reversibility of protein denaturation. Nevertheless, a 100-fold molar excess of the inhibitor led to the incomplete recovery of proteolytic activity, which can be explained by irreversible denaturation. The structural stability of the C-terminal β-sheet rich domain of the papain-like cysteine protease family opens up an interesting possibility to use its foldamers as a strategy for sensor development and other multiple potential applications that rely on the great commercial value of papain-like cysteine proteases.
Language	English
Publishing date	2023-07-01
Publishing country	Switzerland
Document type	Journal Article
ISSN	2313-7673
ISSN (online)	2313-7673
DOI	10.3390/biomimetics8030281
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: One-step purification and freeze stability of papain at acidic pH values

Marković Srđan / Milošević Jelica / Đurić Milica / Lolić Aleksandar / Polović Natalija

Archives of Biological Sciences, Vol 73, Iss 1, Pp 57-

2021 Volume 64

Abstract: Papain is a proteolytic enzyme of great commercial value. It is a cysteine protease highly expressed in Carica papaya fruit latex, but also present in papaya leaves. Purification procedures mostly deal with the latex and include a combination of ... ...

Abstract	Papain is a proteolytic enzyme of great commercial value. It is a cysteine protease highly expressed in Carica papaya fruit latex, but also present in papaya leaves. Purification procedures mostly deal with the latex and include a combination of precipitation and/or chromatographic techniques. Due to its solubility, structure and activity characteristics, the pH and salt content play significant roles in handling papain extracts. Here we report a simple, rapid and easily scalable procedure for papain purification from papaya leaves, which contain different contaminants as compared to papaya latex. Sodium chloride precipitation of contaminants at pH 5 followed by ammonium sulphate precipitation resulted in the removal of other leaf proteins and protein fragments from papain solution and about a 3-fold purification. The procedure also benefits from the suppression of autoproteolysis and preservation of the native structure, as confirmed by FTIR analysis, and the high recovery of activity of over 80%.
Keywords	papain ; papaya leaves ; precipitation techniques ; structural stability ; activity recovery ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2021-01-01T00:00:00Z
Publisher	University of Belgrade, University of Novi Sad
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy.

Milošević, Jelica / Prodanović, Radivoje / Polović, Natalija

Molecules (Basel, Switzerland)

2021 Volume 26, Issue 4

Abstract: Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods ... ...

Abstract	Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis- Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.
MeSH term(s)	Amyloid/chemistry ; Amyloid/ultrastructure ; Amyloidogenic Proteins/chemistry ; Amyloidogenic Proteins/ultrastructure ; Animals ; Benzothiazoles/chemistry ; Chickens ; Fluorescence ; Microscopy, Atomic Force ; Muramidase/chemistry ; Muramidase/ultrastructure ; Protein Structure, Secondary ; Spectroscopy, Fourier Transform Infrared
Chemical Substances	Amyloid ; Amyloidogenic Proteins ; Benzothiazoles ; thioflavin T (2390-54-7) ; hen egg lysozyme (EC 3.2.1.-) ; Muramidase (EC 3.2.1.17)
Language	English
Publishing date	2021-02-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules26040970
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.MO 81: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Using Front-Face Fluorescence Spectroscopy and Biochemical Analysis of Honey to Assess a Marker for the Level of Varroa destructor Infestation of Honey Bee (Apis mellifera) Colonies

Stanković, Mira / Prokopijević, Miloš / Šikoparija, Branko / Nedić, Nebojša / Andrić, Filip / Polović, Natalija / Natić, Maja / Radotić, Ksenija

Foods. 2023 Feb. 02, v. 12, no. 3

2023

Abstract: Varroa destructor is a parasitic mite responsible for the loss of honey bee (Apis mellifera) colonies. This study aimed to find a promising marker in honey for the bee colony infestation level using fluorescence spectroscopy and biochemical analyses. We ... ...

Abstract	Varroa destructor is a parasitic mite responsible for the loss of honey bee (Apis mellifera) colonies. This study aimed to find a promising marker in honey for the bee colony infestation level using fluorescence spectroscopy and biochemical analyses. We examined whether the parameters of the honey samples’ fluorescence spectra and biochemical parameters, both related to proteins and phenolics, may be connected with the level of honey bee colonies’ infestation. The infestation level was highly positively correlated with the catalase activity in honey (r = 0.936). Additionally, the infestation level was positively correlated with the phenolic spectral component (r = 0.656), which was tentatively related to the phenolics in honey. No correlation was found between the diastase activity in honey and the colonies’ infestation level. The results indicate that the catalase activity in honey and the PFC1 spectral component may be reliable markers for the V. destructor infestation level of the colonies. The obtained data may be related to the honey yield obtained from the apiaries.
Keywords	Apis mellifera ; Varroa destructor ; amylases ; catalase ; fluorescence ; fluorescence emission spectroscopy ; honey ; honey bees ; parasitic mites ; phenolic compounds
Language	English
Dates of publication	2023-0202
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article ; Online
ZDB-ID	2704223-6
ISSN	2304-8158
ISSN	2304-8158
DOI	10.3390/foods12030629
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article: Using Front-Face Fluorescence Spectroscopy and Biochemical Analysis of Honey to Assess a Marker for the Level of

Stanković, Mira / Prokopijević, Miloš / Šikoparija, Branko / Nedić, Nebojša / Andrić, Filip / Polović, Natalija / Natić, Maja / Radotić, Ksenija

Foods (Basel, Switzerland)

2023 Volume 12, Issue 3

Abstract: ... Varroa ... ...

Abstract	Varroa destructor
Language	English
Publishing date	2023-02-02
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704223-6
ISSN	2304-8158
ISSN	2304-8158
DOI	10.3390/foods12030629
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure

Mijin Nemanja D. / Milošević Jelica / Filipović Nenad R. / Mitić Dragana / Anđelković Katarina / Polović Natalija Đ. / Todorović Tamara R.

Journal of the Serbian Chemical Society, Vol 87, Iss 10, Pp 1143-

2022 Volume 1156

Abstract: Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancer cell lines were investigated. However, the results of the cytotoxic activity did not correlate with the ... ...

Abstract	Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancer cell lines were investigated. However, the results of the cytotoxic activity did not correlate with the hydrophobic character of the complexes. To gain further insight into the structure–activity relationship, essential for the design of novel potential drugs, other factors, such as non-specific interactions with cellular proteins, have to be taken into account. To explore the potential non-specific influence of the complexes on protein structures, ovalbumin (OVA) was chosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold. Contrary, the effect of complex 5 on OVA secondary structures was concentration- dependent. While the lower concentration of complex 5 had no effect on OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water may be related to a potential crosslinking that leads to OVA aggregation.
Keywords	ovalbumin model system ; protein aggregation ; dmso effect ; ligand hydrophobicity ; Chemistry ; QD1-999
Subject code	500
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Serbian Chemical Society
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans

Dragačević, Luka / Lopandić, Zorana / Gavrović-Jankulović, Marija / Živković, Irena / Blagojević, Veljko / Polović, Natalija / Minić, Rajna

Applied biochemistry and biotechnology. 2022 May, v. 194, no. 5

2022

Abstract: The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine ...

Abstract	The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA₁₂₀), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA₁₂₀. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.
Keywords	Musa acuminata ; Ricinus communis ; biotechnology ; flow cytometry ; green fluorescent protein ; lectins ; polysaccharides ; sorbents
Language	English
Dates of publication	2022-05
Size	p. 2047-2060.
Publishing place	Springer US
Document type	Article
ZDB-ID	392344-7
ISSN	0273-2289
ISSN	0273-2289
DOI	10.1007/s12010-021-03772-w
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 80/718: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article: Dopamine-modified pectin for a Streptomyces cyaneus laccase induced microbeads formation, immobilization, and textile dyes decolorization

Popović, Nikolina / Stanišić, Marija / Ilić Đurđić, Karla / Prodanović, Olivera / Polović, Natalija / Prodanović, Radivoje

Environmental technology & innovation. 2021 May, v. 22

2021

Abstract: Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium ... ...

Abstract	Pectins are a group of heterologous polysaccharides capable of forming hydrogels and applicable in many industrial processes. A new type of modified pectin was synthesized by periodate oxidation and reductive amination with dopamine and sodium cyanoborohydride. The success of modification was confirmed by UV–Vis,FTIR, and ¹H NMR spectroscopy. The obtained dopamine-pectin could form hydrogels by ionic crosslinking of carboxyl groups with calcium or by crosslinking phenol groups with laccase. For enzymatic crosslinking with laccase from Streptomyces cyaneus expressed in E. coli, isolation and purification of the enzyme was done. Using emulsion-based enzymatic crosslinking polymerization, dopamine-pectin microbeads with immobilized laccase were made. The immobilized laccase showed improved thermal and pH stability in comparison to the free enzyme. The immobilized biocatalyst effectively decolorized various dyes: Amido Black 10B, Reactive Black 5, and Evans Blue. After ten cycles of repeated use, the microbead immobilized laccase could still decolorize 60% and 36% of Amido Black 10B and Reactive Black 5, respectively.
Keywords	Escherichia coli ; Streptomyces cyaneus ; amination ; biocatalysts ; calcium ; crosslinking ; decolorization ; dopamine ; environmental technology ; fabrics ; hydrogels ; laccase ; microbeads ; nuclear magnetic resonance spectroscopy ; oxidation ; pH stability ; pectins ; phenol ; polymerization ; sodium
Language	English
Dates of publication	2021-05
Publishing place	Elsevier B.V.
Document type	Article
Note	NAL-AP-2-clean
ISSN	2352-1864
DOI	10.1016/j.eti.2021.101399
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article: Optimization of phenol removal with horseradish peroxidase encapsulated within tyramine-alginate micro-beads

Pantić, Nevena / Prodanović, Radivoje / Đurđić, Karla Ilić / Polović, Natalija / Spasojević, Milica / Prodanović, Olivera

Environmental technology & innovation. 2021 Feb., v. 21

2021

Abstract: Removal of phenolic compounds from water is of major interest over the years, since they are one of the most common pollutants in aqueous systems. Horseradish peroxidase (HRP) is the most investigated biocatalyst for this purpose. Inactivation of the ... ...

Abstract	Removal of phenolic compounds from water is of major interest over the years, since they are one of the most common pollutants in aqueous systems. Horseradish peroxidase (HRP) is the most investigated biocatalyst for this purpose. Inactivation of the enzyme is a major issue which can be successfully overcome by the enzyme immobilization on different polymers. In this study, tyramine-alginate micro-beads were used as carriers for the immobilization of horseradish peroxidase. The effect of the oxidation degree of tyramine-alginates on a specific activity of the enzyme was tested. An increase in the concentration of oxidized alginate from 2.5 to 20% resulted in a gradual increase in the specific activity from 0.05 to 0.67 U/mL. HRP immobilized within these micro-beads was tested for the phenol removal in a batch reactor. Reaction conditions were optimized to achieve a high removal efficiency and substantial reusability of the system. In this study, for the first time, an internal generation of hydrogen peroxide from glucose and glucose oxidase was employed in the phenol removal process with HRP immobilized on tyramine-alginate. Within 6 h of repeated use 96% of phenol was removed when the system for internal delivery of H₂O₂, composed of 0.187 U/mL of glucose oxidase and 4 mmol/L of glucose was employed. A common straightforward addition of hydrogen peroxide provided the removal efficiency of only 42%, under the same reaction conditions. The highest efficiency of the phenol removal (96%) was obtained with HRP immobilized within 20 mol% oxidized tyramine-alginate micro-beads. Fifteen mol% oxidized tyramine-alginate showed lower removal efficiency in the first cycle of use (73%) but more promising reusability, since the immobilized enzyme retained 61% of its initial activity even after four consecutive cycles of use.
Keywords	alginates ; batch systems ; biocatalysts ; environmental technology ; enzyme activity ; glucose ; glucose oxidase ; hydrogen peroxide ; hydrogen production ; immobilized enzymes ; microbeads ; oxidation ; peroxidase ; phenol
Language	English
Dates of publication	2021-02
Publishing place	Elsevier B.V.
Document type	Article
Note	NAL-AP-2-clean
ISSN	2352-1864
DOI	10.1016/j.eti.2020.101211
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article: Comparative stability of ficin and papain in acidic conditions and the presence of ethanol

Milošević, Jelica / Janković, Brankica / Polović, Natalija / Prodanović, Radivoje

Amino acids. 2019 May, v. 51, no. 5

2019

Abstract: Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic–alcoholic conditions is well-characterized ... ...

Abstract	Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic–alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic–acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.
Keywords	alcoholic beverages ; beverage industry ; cold ; cold storage ; denaturation ; ethanol ; ficain ; Fourier transform infrared spectroscopy ; papain ; peptides ; pH ; proteolysis ; storage quality ; substrate specificity
Language	English
Dates of publication	2019-05
Size	p. 829-838.
Publishing place	Springer Vienna
Document type	Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-019-02724-3
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 3490: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

To top

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito