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1. Influence of pH and ionic strength on the thermal gelation behaviour of pea protein

Author:
Tanger, Caren; Müller, Michaela; Andlinger, David; Kulozik, Ulrich
Source:
Food hydrocolloids 2022 v.123 pp. 106903
ISSN:
0268-005X
Subject:
denaturation,   etc   ; gelatinization temperature; gelation; gels; heat; hydrocolloids; hydrophobicity; ionic strength; modulus of elasticity; pH; pea protein; rheology; solubility; thermal properties;     Show all 14 Subjects
Abstract:
... Gelation is one of the functional properties of protein, which can be controlled by pH and ionic strength. However, kowledge related to gelation properties of emerging plant proteins is still limited. In this paper, the solubility, the thermal behaviour and gelation behaviour of pea protein were analysed. Gels were analysed rheologically measuring the elastic modulus G′₂₅°C, the ratio of G′₂₅°C to ...
DOI:
10.1016/j.foodhyd.2021.106903

2. The binding of different model membranes with PKCε C2 domain is not dependent on membrane curvature but affects the sequence of events during unfolding

Author:
Ausili, Alessio; Corbalán-García, Senena; Gómez-Fernández, Juan C.
Source:
Archives of biochemistry and biophysics 2021 v.705 pp. 108910
ISSN:
0003-9861
Subject:
denaturation,   etc   ; biophysics; cardiolipins; lysophosphatidylcholine;     Show all 4 Subjects
Abstract:
... The C2 domain of novel protein kinases C (nPKC) binds to membranes in a Ca²⁺-independent way contributing to the activation of these enzymes. We have studied the C2 domain of one of these nPKCs, namely PKCε, and confirmed that it establishes a strong interaction with POPA, which is clearly visible through changes in chemical shifts detected through ³¹P-MAS-NMR and the protection that it exerts on ...
DOI:
10.1016/j.abb.2021.108910

3. Concentration-dependent changes in the reaction behavior of whey proteins: Diffusion-controlled or transition state-controlled reactions?

Author:
Quevedo, Maria; Karbstein, Heike P.; Emin, M. Azad
Source:
Food hydrocolloids 2021 v.118 pp. 106745
ISSN:
0268-005X
Subject:
denaturation; protein denaturation,   etc   ; hydrocolloids; meat; mechanical methods; whey; whey protein;     Show all 7 Subjects
Abstract:
... The denaturation of whey proteins can be used in a controlled manner to design protein-based products with new specific structures or functionalities e.g., meat and dairy analogues, as well as protein-based emulsifiers and thickeners with specific functionalities. For this, the influence of thermal and/or mechanical treatment, and milieu conditions including the protein concentration, on the denat ...
DOI:
10.1016/j.foodhyd.2021.106745

4. Comparing different methods for estimating kinetic parameters of whey protein heat-induced denaturation in infant milk formulas

Author:
Leite, Bruno; Croguennec, Thomas; Halabi, Amira; Costa Junior, Esly Ferreira da
Source:
Journal of food engineering 2021 v.292 pp. 110272
ISSN:
0260-8774
Subject:
denaturation; protein denaturation,   etc   ; lactoferrin; least squares; milk; variance; whey protein;     Show all 7 Subjects
Abstract:
... Modeling the heat-induced denaturation of milk proteins is a relevant issue because of heating processes in the manufacturing of several dairy products. In this study, four different parameter estimation methods were evaluated to estimate the kinetic parameters of the heat-induced protein denaturation of β-lactoglobulin (β-LG) and lactoferrin (LF) in infant milk formulas (IMF). The methods were: a ...
DOI:
10.1016/j.jfoodeng.2020.110272

5. Cryogenic activity and stability of benzaldehyde lyase enzyme in lipidic mesophases-nanoconfined water

Author:
Zhou, Tao; Yao, Yang; Zhang, Qin; Mezzenga, Raffaele
Source:
Chemical communications 2021 v.57 no.46 pp. 5650-5653
ISSN:
1364-548X
Subject:
denaturation,   etc   ; benzaldehyde; cold; enzymes; liquids;     Show all 5 Subjects
Abstract:
... Phytantriol-based lipidic mesophases (LMs) are introduced as a platform for cryoenzymology, which relies on the presence of liquid water in LMs at subzero temperatures. After incorporation into LMs, the model enzyme Benzaldehyde lyase (BAL) shows high cryogenic stability and activity. In contrast, BAL in bulk solution undergoes significant secondary structural transitions caused by low temperature ...
DOI:
10.1039/d1cc01315g

6. Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions

Author:
Sahin, Cagla; Österlund, Nicklas; Leppert, Axel; Johansson, Jan; Marklund, Erik G.; Benesch, Justin L. P.; Ilag, Leopold L.; Allison, Timothy M.; Landreh, Michael
Source:
Chemical communications 2021 v.57 no.12 pp. 1450-1453
ISSN:
1364-548X
Subject:
protein denaturation,   etc   ; mass spectrometry; pH;     Show all 3 Subjects
Abstract:
... Although native mass spectrometry is widely applied to monitor chemical or thermal protein denaturation, it is not clear to what extent it can inform about alkali-induced unfolding. Here, we probe the relationship between solution- and gas-phase structures of proteins under alkaline conditions. Native ion mobility-mass spectrometry reveals that globular proteins are destabilized rather than global ...
DOI:
10.1039/d0cc08135c

7. Effects of Ionic Liquids on Aqueous Urea Solutions: Insights into the Ionic Liquid-Assisted Protein Renaturation

Author:
Rahman, Mohammad Homaidur; Senapati, Sanjib
Source:
TheJournal of physical chemistry 2021 v.125 no.18 pp. 4808-4818
ISSN:
1520-5207
Subject:
protein denaturation,   etc   ; molecular dynamics; nitrates; peptides; urea;     Show all 5 Subjects
Abstract:
... Ionic liquids (ILs) are designer solvents that find wide applications in various areas. Recently, ILs have been shown to induce the refolding of certain proteins that were previously denatured under the treatment of urea. A molecular-level understanding of the counteracting mechanism of ILs on urea-induced protein denaturation remains elusive. In this study, we employ atomistic molecular dynamics ...
DOI:
10.1021/acs.jpcb.1c00586

8. A novel F30S mutation in γS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses

Author:
Wang, Kai-Jie; Liao, Xiao-Yan; Lin, Kunxia; Xi, Yi-Bo; Wang, Sha; Wan, Xiu-Hua; Yan, Yong-Bin
Source:
International journal of biological macromolecules 2021 v.172 pp. 475-482
ISSN:
0141-8130
Subject:
denaturation,   etc   ; cataract; genetic variation; mutation; phenotype; spectroscopy;     Show all 6 Subjects
Abstract:
... Despite of increasingly accumulated genetic variations of autosomal dominant congenital cataracts (ADCC), the causative genes of many ADCC patients remains unknown. In this research, we identified a novel F30S mutation in γS-crystallin from a three-generation Chinese family with ADCC. The patients possessing the F30S mutation exhibited nuclear cataract phenotype. The potential molecular mechanism ...
DOI:
10.1016/j.ijbiomac.2021.01.079

9. Polyanions Cause Protein Destabilization Similar to That in Live Cells

Author:
Sörensen, Therese; Leeb, Sarah; Danielsson, Jens; Oliveberg, Mikael
Source:
Biochemistry 2021 v.60 no.10 pp. 735-746
ISSN:
1520-4995
Subject:
denaturation,   etc   ; anions; nuclear magnetic resonance spectroscopy; nucleotides;     Show all 4 Subjects
Abstract:
... The structural stability of proteins is found to markedly change upon their transfer to the crowded interior of live cells. For some proteins, the stability increases, while for others, it decreases, depending on both the sequence composition and the type of host cell. The mechanism seems to be linked to the strength and conformational bias of the diffusive in-cell interactions, where protein char ...
DOI:
10.1021/acs.biochem.0c00889

10. PCR procedures to amplify GC-rich DNA sequences of Mycobacterium bovis

Author:
Assal, Nadia; Lin, Min
Source:
Journal of microbiological methods 2021 v.181 pp. 106121
ISSN:
0167-7012
Subject:
denaturation,   etc   ; DNA; Listeria monocytogenes; Mycobacterium bovis; genes;     Show all 5 Subjects
Abstract:
... Amplification of high GC content genes by PCR is a major challenge during the creation of recombinant GC-rich DNA constructs. This may be due to the difficulty in DNA denaturation or the possibility of forming secondary structures from DNA templates. Tools have been described to address the technical problems associated with the amplification of shorter sequences (<1000 bp). However, obstacles of ...
DOI:
10.1016/j.mimet.2020.106121

11. Parchment Browning–part II: The Dead Sea Scrolls

Author:
Maor, Yonah; Shor, Pnina; Aizenshtat, Zeev
Source:
Polymer degradation and stability 2021 v.183 pp. 109414
ISSN:
0141-3910
Subject:
denaturation,   etc   ; archaeology; degradation; hydrolysis; melanoidins; saline water;     Show all 6 Subjects
Abstract:
... The Dead Sea Scrolls are often described as the most important archaeological find of the 20th century. These 2000 years old manuscripts have great religious, historical and linguistic importance. The fact that large parts of these texts are obscured by the darkening of the parchment is extremely unfortunate. In our previous research we explored the possible causes of parchment browning or darkeni ...
DOI:
10.1016/j.polymdegradstab.2020.109414

12. Myosin sensitivity to thermal denaturation explains differences in water loss and shrinkage during cooking in muscles of distinct fibre types

Author:
Vaskoska, Rozita; Ha, Minh; Ong, Lydia; Chen, George; White, Jason; Gras, Sally; Warner, Robyn
Source:
Meat science 2021 v.179 pp. 108521
ISSN:
0309-1740
Subject:
denaturation; protein denaturation,   etc   ; collagen; enthalpy; homogenization; meat science; muscles; myosin; pH; sarcomeres; shrinkage; temperature; water content;     Show all 13 Subjects
Abstract:
... The effect of thermal protein denaturation on the structure and quality of muscles of different fibre types is not well understood. Unaged masseter (100% type I fibres) and cutaneous trunci (93% type II fibres) muscles (N = 10) were assessed for their characteristics, protein denaturation, cooking loss, Warner- Bratzler shear force (WBSF) and shrinkage after heating at 50 °C - 85 °C with a rate of ...
DOI:
10.1016/j.meatsci.2021.108521

13. Effect of pH and urea on the proteins secondary structure at the water/air interface and in solution

Author:
Guckeisen, Tobias; Hosseinpour, Saman; Peukert, Wolfgang
Source:
Journal of colloid and interface science 2021 v.590 pp. 38-49
ISSN:
0021-9797
Subject:
denaturation; protein denaturation,   etc   ; air; circular dichroism spectroscopy; hydrophobicity; liquids; pH; urea;     Show all 8 Subjects
Abstract:
... The secondary structure of proteins affects their functionality and performance in physiological environments or industrial applications. Change of the solution pH or the presence of protein denaturants are the main chemical means that can alter the secondary structure of proteins or lead to protein denaturation. Since proteins in the bulk solution and those residing at the solution/air interface ...
DOI:
10.1016/j.jcis.2021.01.015

14. Influence of chaperone-like activity of caseinomacropeptide on the gelation behaviour of whey proteins at pH 6.4 and 7.2.

Author:
Gaspard, Sophie J.; Sharma, Prateek; Fitzgerald, Ciarán; Tobin, John T.; O’Mahony, James A.; Kelly, Alan L.; Brodkorb, André
Source:
Food hydrocolloids 2021 v.112 pp. 106249
ISSN:
0268-005X
Subject:
denaturation; protein denaturation,   etc   ; confocal microscopy; gelatinization temperature; gelation; gels; hydrocolloids; pH; rheology; whey; whey protein;     Show all 11 Subjects
Abstract:
... The effect of caseinomacropeptide (CMP) on the heat-induced denaturation and gelation of whey proteins (2.5–10%, w/v) at pH 6.4 and 7.2, at a whey protein:CMP ratio of 1:0.9 (w/w), was investigated using differential scanning calorimetry (DSC), oscillatory rheology (90 °C for 20 min) and confocal microscopy. Greater frequency-dependence in the presence of CMP suggested that the repulsive interacti ...
DOI:
10.1016/j.foodhyd.2020.106249

15. Effects of Frozen Storage Temperature and Duration on Changes in Physicochemical Properties of Beef Myofibrillar Protein

Author:
Qian, Shuyi; Li, Xia; Wang, Hang; Mehmood, Waris; Zhang, Chunhui; Blecker, Christophe
Source:
Journal of food quality 2021 v.2021
ISSN:
1745-4557
Subject:
denaturation; protein denaturation,   etc   ; ; beef; food quality; frozen storage; hydrogen; hydrophobicity; storage temperature; storage time;     Show all 10 Subjects
Abstract:
... This study aimed to address the effects of frozen storage temperature and duration on the changes in physicochemical properties of beef myofibrillar protein. The beef was stored at −1, −6, −9, −12, and −18°C for 28, 84, 126, 168, and 168 days, respectively. The myofibrillar protein of beef samples denatured gradually with the extention of storage period. Regarding the samples stored at temperature ...
DOI:
10.1155/2021/8836749

16. Impacts of high pressure assisted freezing on the denaturation of polyphenol oxidase

Author:
Cheng, Lina; Zhu, Zhiwei; Sun, Da-Wen
Source:
Food chemistry 2021 v.335 pp. 127485
ISSN:
0308-8146
Subject:
denaturation; protein denaturation,   etc   ; catechol oxidase; crystallization; enzyme activity; food chemistry; ice; mushrooms; pressure; temperature; thermodynamics;     Show all 11 Subjects
Abstract:
... The mechanism of enzyme protein denaturation induced by high pressure freezing is complicated and unclear as this process involves Pressure-Factors (pressure and time) and Freezing-Factors (temperature, phase transition, recrystallization, and ice crystal types). In this study, the thermodynamics and conformation changes of mushroom polyphenol oxidase (PPO) under high pressure freezing treatments ...
DOI:
10.1016/j.foodchem.2020.127485

17. Biomimetic electrochemical sensors: New horizons and challenges in biosensing applications

Author:
Romanholo, Pedro V.V.; Razzino, Claudia A.; Raymundo-Pereira, Paulo A.; Prado, Thiago M.; Machado, Sergio A.S.; Sgobbi, Livia F.
Source:
Biosensors & bioelectronics 2021 v.185 pp. 113242
ISSN:
0956-5663
Subject:
protein denaturation,   etc   ; biomimetics; biosensors; electrochemistry; markets; molecular imprinting;     Show all 6 Subjects
Abstract:
... The urge to meet the ever-growing needs of sensing technology has spurred research to look for new alternatives to traditional analytical methods. In this scenario, the glucometer is the flagship of commercial electrochemical sensing platforms, combining selectivity, reliability and portability. However, other types of enzyme-based biosensors seldom achieve the market, in spite of the large and in ...
DOI:
10.1016/j.bios.2021.113242

18. Reversibility and irreversibility in the temperature denaturation of monoclonal antibodies

Author:
Schön, Arne; Freire, Ernesto
Source:
Analytical biochemistry 2021 v.626 pp. 114240
ISSN:
0003-2697
Subject:
denaturation,   etc   ; biochemistry; heat; models; monoclonal antibodies; pH; temperature; therapeutics; viability;     Show all 9 Subjects
Abstract:
... There have been numerous studies of the temperature denaturation of monoclonal antibodies (mAbs) using differential scanning calorimetry (DSC). In general, mAbs are characterized by complex temperature denaturation transitions in which the various domains (CH2, CH3, Fab) give rise to different peaks in the heat capacity function. The complexity and overall irreversibility of the temperature denatu ...
DOI:
10.1016/j.ab.2021.114240

19. Peptide-MHC I complex stability measured by nanoscale differential scanning fluorimetry reveals molecular mechanism of thermal denaturation

Author:
Saikia, Ankur; Springer, Sebastian
Source:
Molecular immunology 2021 v.136 pp. 73-81
ISSN:
0161-5890
Subject:
denaturation,   etc   ; fluorescence; fluorometry; immunotherapy; major histocompatibility complex; peptides; tryptophan;     Show all 7 Subjects
Abstract:
... Recombinant major histocompatibility complex class I molecules are used in diagnostic and therapeutic approaches in cancer immunotherapy, with many studies exploring their binding to antigenic peptides. Current techniques for kinetic peptide binding studies are hampered by high sample consumption, low throughput, interference with protein stability, and/or high background signal. Here, we validate ...
DOI:
10.1016/j.molimm.2021.04.028

20. Osmolyte-Induced Effects on the Hydration Behavior and the Osmotic Second Virial Coefficients of Alkyl-Substituted Urea Derivatives: Critical Assessment of Their Structure-Making/Breaking Behavior

Author:
Chialvo, Ariel A.; Crisalle, Oscar D.
Source:
TheJournal of physical chemistry 2021 v.125 no.23 pp. 6231-6243
ISSN:
1520-5207
Subject:
denaturation,   etc   ; Gibbs free energy; microstructure; solvation; temperature; urea;     Show all 6 Subjects
Abstract:
... We analyzed the hydration behavior of alkyl-substituted urea osmolytes in terms of their deviation from Lewis–Randall solution ideality and characterized their structure-making/breaking tendency according to a proposed solvation formalism that provides a rigorous cause–effect connection between the system microstructure and its solution thermodynamic nonidealities. After a brief introduction of th ...
DOI:
10.1021/acs.jpcb.1c01855