scholarly journals Protein thermal stabilization in aqueous solutions of osmolytes.

2015 ◽  
Vol 63 (1) ◽  
Author(s):  
Piotr Bruździak ◽  
Aneta Panuszko ◽  
Muriel Jourdan ◽  
Janusz Stangret
Keyword(s):  
Thermal Stability ◽  
Aqueous Solutions ◽  
Theoretical Calculations ◽  
Thermal Stabilization ◽  
Protein Stabilization ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Thermal Stability Of ◽  
Distinctive Role

Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N,N,N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spectroscopic investigation were compared with FTIR hydration studies' results. Selected osmolytes increased lysozyme's thermal stability in the following order: Gly>NMG>TMAO≈DMG>TMG. Theoretical calculations (DFT) showed clearly that osmolytes' amino group protons and water molecules interacting with them played a distinctive role in protein thermal stabilization. The results brought us a step closer to the exact mechanism of protein stabilization by osmolytes.

Influence of tyrosine nitration on the structure and thermal stability of hen egg white lysozyme

Nitric Oxide ◽  
2012 ◽  
Vol 27 ◽  
pp. S37-S38
Author(s):  
Maria Gómez-Mingot ◽  
Luis A. Alcaraz ◽  
Antonio Donaire ◽  
Jesús Iniesta ◽  
Vicente Montiel
Keyword(s):  
Thermal Stability ◽  
Egg White ◽  
Tyrosine Nitration ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Thermal Stability Of ◽  
Hen Egg

scholarly journals Structural insights into protein folding, stability and activity using in vivo perdeuteration of hen egg-white lysozyme

IUCrJ ◽  
2021 ◽  
Vol 8 (3) ◽  
Author(s):  
Joao Ramos ◽  
Valerie Laux ◽  
Michael Haertlein ◽  
Elisabetta Boeri Erba ◽  
Katherine E. McAuley ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Enzymatic Function ◽  
Biophysical Study ◽  
Hen Egg White ◽  
Thermal Stability Of ◽  
Hen Egg

This structural and biophysical study exploited a method of perdeuterating hen egg-white lysozyme based on the expression of insoluble protein in Escherichia coli followed by in-column chemical refolding. This allowed detailed comparisons with perdeuterated lysozyme produced in the yeast Pichia pastoris, as well as with unlabelled lysozyme. Both perdeuterated variants exhibit reduced thermal stability and enzymatic activity in comparison with hydrogenated lysozyme. The thermal stability of refolded perdeuterated lysozyme is 4.9°C lower than that of the perdeuterated variant expressed and secreted in yeast and 6.8°C lower than that of the hydrogenated Gallus gallus protein. However, both perdeuterated variants exhibit a comparable activity. Atomic resolution X-ray crystallographic analyses show that the differences in thermal stability and enzymatic function are correlated with refolding and deuteration effects. The hydrogen/deuterium isotope effect causes a decrease in the stability and activity of the perdeuterated analogues; this is believed to occur through a combination of changes to hydrophobicity and protein dynamics. The lower level of thermal stability of the refolded perdeuterated lysozyme is caused by the unrestrained Asn103 peptide-plane flip during the unfolded state, leading to a significant increase in disorder of the Lys97–Gly104 region following subsequent refolding. An ancillary outcome of this study has been the development of an efficient and financially viable protocol that allows stable and active perdeuterated lysozyme to be more easily available for scientific applications.

scholarly journals Thermal Stabilization of HEWL by Adsorption on Biochar

2019 ◽  
Vol 8 (4) ◽  
pp. 30
Author(s):  
Hidetaka Noritomi ◽  
Ryotaro Kai ◽  
Nobuyuki Endo ◽  
Satoru Kato ◽  
Katsumi Uchiyama
Keyword(s):  
Heat Stress ◽  
Secondary Structure ◽  
Thermal Stabilization ◽  
Egg White ◽  
Bamboo Charcoal ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Heat Stress Tolerance ◽  
Hen Egg White ◽  
Hen Egg

We have found that the heat stress tolerance of hen egg white lysozyme (HEWL) is markedly enhanced by the adsorption of HEWL on bamboo charcoal powder (BCP), which is a kind of biochar. HEWL was firmly adsorbed on BCP even at high temperatures. The secondary structure of HEWL was altered to some extent by the adsorption of HEWL on BCP. The remaining activity of BCP-adsorbed HEWL exhibited more than 20% after the incubation for 30 min at 900C although that of free one was hardly observed. Moreover, the half-life of BCP-adsorbed HEWL was 13 min at 900C while that of free one was 4 min.

The influence of maltose modified poly(propylene imine) dendrimers on hen egg white lysozyme structure and thermal stability

2012 ◽  
Vol 95 ◽  
pp. 103-108 ◽  
Author(s):  
Michal Ciolkowski ◽  
Bartłomiej Pałecz ◽  
Dietmar Appelhans ◽  
Brigitte Voit ◽  
Barbara Klajnert ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Poly Propylene ◽  
Hen Egg

Inactivation of hen egg-white lysozyme. The azide radical

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

The inhibitory role of clioquinol in the fibrillation of hen egg white lysozyme

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Inhibitory Role ◽  
Hen Egg White ◽  
Hen Egg
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