Effect of sulfoxides on the thermal denaturation of hen lysozyme: A calorimetric and Raman study

Torreggiani, Armida; Foggia, Michele Di; Manco, Immacolata; Maio, Anna De; Markarian, Shiraz A.; Bonora, Sergio

doi:10.1016/j.molstruc.2008.03.007

Cited by 50 publications

(42 citation statements)

References 35 publications

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“…Therapeutic proteins may rapidly denature and lose their enzymatic activity. The structure changes detected using FT-Raman and the absence of Tm detected by DSC have been used to monitor the denaturation of proteins, and the results of Raman and DSC are linked to the results of enzymatic activity [34]. Our DSC and Raman results confirmed the denaturation of both 301 proteins studied.…”

Section: Enzymatic Assaysupporting

confidence: 58%

Effect of mechanical denaturation on surface free energy of protein powders

Mohammad

Grimsey

Forbes

et al. 2016

Colloids and Surfaces B: Biointerfaces

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47Globular proteins are important both as therapeutic agents and excipients. However, their fragile 48 native conformations can be denatured during pharmaceutical processing, which leads to 49 modification of the surface energy of their powders and hence their performance. Lyophilized 50 powders of hen egg-white lysozyme and β-galactosidase from Aspergillus oryzae were used as 51 models to study the effects of mechanical denaturation on the surface energies of basic and 52 acidic protein powders, respectively. Their mechanical denaturation upon milling was confirmed 53by the absence of their thermal unfolding transition phases and by the changes in their secondary 54 and tertiary structures. Inverse gas chromatography detected differences between both 55 unprocessed protein powders and the changes induced by their mechanical denaturation. The 56 surfaces of the acidic and basic protein powders were relatively basic, however the surface 57 acidity of β-galactosidase was higher than that of lysozyme. Also the surface of β-galactosidase 58 powder had a higher dispersive energy compared to lysozyme. The mechanical denaturation 59 decreased the dispersive energy and the basicity of the surfaces of both protein powders. The 60 amino acid composition and molecular conformation of the proteins explained the surface energy 61 data measured by inverse gas chromatography. The biological activity of mechanically denatured 62 protein powders can either be reversible (lysozyme) or irreversible (β-galactosidase) upon 63 hydration. Our surface data can be exploited to understand and predict the performance of 64 protein powders within pharmaceutical dosage forms. 65 66

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Section: Enzymatic Assaysupporting

confidence: 58%

Effect of mechanical denaturation on surface free energy of protein powders

Mohammad

Grimsey

Forbes

et al. 2016

Colloids and Surfaces B: Biointerfaces

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“…Thermal processing is mandatory for food preparation, especially for muscle foods. The degree of denaturation of these foods is significantly correlated with time and temperature applied (Torreggiani and others ). Mild heating (60 to 80 °C) induces denaturation of myofibrillar proteins and collagen, resulting in enhanced accessibility of gastrointestinal proteases (Bax and others ).…”

Section: Introductionmentioning

confidence: 99%

Chemical and Cellular Antioxidant Activities of Chicken Breast Muscle Subjected to Various Thermal Treatments Followed by Simulated Gastrointestinal Digestion

Sangsawad

Kiatsongchai

Chitsomboon

et al. 2016

Journal of Food Science

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The effect of thermal treatments on chemical and cellular antioxidant activities of chicken breasts subjected to in vitro gastrointestinal digestion was investigated. Breast of Korat crossbred chicken (KC) and commercial broiler (BR) were cooked under various conditions, namely heating at 70 °C for 30 min (H-0.5) and 24 h (H-24), autoclaving (AC) at 121°C for 15 min (AC-15) and 60 min (AC-60). Protein digestibility decreased upon the extreme thermal treatment of AC-60. The H-0.5 improved metal chelating activity of KC digesta, FRAP, and anti-liposome oxidation of BR digesta. Digesta of BR/H-0.5 and KC/AC-15 at 50 μg/mL exhibited the highest cytoprotective effect against tert-butyl hydroperoxide (TBHP)-induced oxidative damage of HepG2 cells. In addition, the KC/AC-15 digesta at a concentration as low as 12.5 μg/mL inhibited intracellular TBHP-induced reactive oxyfen species (ROS) production (P < 0.05). Thus, the digesta of KC breasts subjected to AC-15 provides not only nutritional value but also antioxidant activity at the cellular level.

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“…The degree of denaturation is highly related to the treatment time and temperature applied (Torreggiani et al, 2008). Thermal modification is often used to facilitate the enzymatic hydrolysis of proteins.…”

Section: Introductionmentioning

confidence: 99%