A detailed analysis of the influence of β-cyclodextrin derivates on the thermal denaturation of lysozyme

Change in the Kinetic Regime of Aggregation of Yeast Alcohol Dehydrogenase in the Presence of 2-Hydroxypropyl-β-cyclodextrin

“…Therefore, this chemical chaperone did not prevent the thermal unfolding of the protein molecule (Scheme 1, line 1), and its protective effect was manifested at subsequent stages of the aggregation process. Similar data were obtained for rabbit skeletal muscle creatine kinase [41] and lysozyme [42]: 2-HP-β-CD did not prevent the protein denaturation, but slowed down its aggregation.…”

“…It includes the interaction of cyclodextrin with the Phe110 residue in the denatured intermediate and, therefore, decreasing the ability of the latter to form aggregates by consequent polymerization. A similar version was proposed by Starciuc et al [42], according to which HP-β-CD destabilizes the tertiary structure of lysozyme under heat stress, increasing the flexibility of the protein and causing destabilization of its secondary structure, and inhibition of lysozyme aggregation is associated with the ability of HP-β-CD to form an inclusion complex with the protein and prevent the formation of new strong H-bonds between β-sheet structures. We can suppose that a similar mechanism can be realized in our case for yADH p and 2-HP-β-CD, especially considering the change in the kinetics of the initial aggregation stage from bimolecular to more complex.…”

Effect of Chemical Chaperones on the Stability of Proteins during Heat– or Freeze–Thaw Stress

“…This is not the only known case when cyclodextrins destabilize proteins. HPCD promotes the destabilization and aggregation of glyceraldehyde-3-phosphate dehydrogenase [ 30 ] or lysozyme [ 28 ]. In some cases, high and low concentrations of HPCD have different effects on the stability of the same protein.…”

“…HPCD can inhibit protein aggregation at air-water, ice-water interfaces during freeze–thawing, exhibiting similarities with surfactants action [ 24 ]. In some cases, HPCD can provoke protein destabilization and accelerate their thermal denaturation and aggregation [ 28 , 29 , 30 ].…”

Determination of conformational changes of polyphenol oxidase and peroxidase in peach juice during mild heat treatment using FTIR spectroscopy coupled with chemometrics

“…Although FTIR spectroscopy was used for the determination of structural changes in enzymes such as mushroom PPO, there has been no study on the determination of the change in secondary structures of peach PPO and POD enzymes during thermal treatment by FTIR spectroscopy with chemometrics. The combined use of chemometric methods (principle component analysis; PCA and partial least square; PLS) and IR spectroscopies is a good alternative for the discrimination and prediction of the structural alterations of the enzyme and proteins (Navea et al ., 2006; Starciuc et al ., 2019). The PLS calibration models were constructed to investigate and validate the IR as an alternative technique for the analysis of secondary structure in different proteins and enzymes (Wang et al ., 2008; Wilcox et al ., 2016; Lopes et al ., 2020).…”