Investigating variables and mechanisms that influence protein integrity in low water content amorphous carbohydrate matrices

How foam stability against drainage is affected by conditions of prior whey protein powder storage and dry-heating: A multidimensional experimental approach

“…Indeed, lactose improved foam stability at pH 3.5 but decreased it at pH 6.5 and a w 0.52. Consistently, pH effects on protein powder glycation have already been observed (Povey et al, 2009;Thomsen et al, 2012).…”

“…Dry-heating of egg white powder is commonly applied to maintain the microbiological quality and improve foaming and gelling properties (Boreddy et al, 2016). In comparison with heating of liquid solutions, dry-heating of protein powders is a way to disconnect proteins denaturation and aggregation and also to obtain different protein structural modifications (Desfougères et al, 2011;Gulzar et al, 2011;Povey et al, 2009). Indeed, Desfougères et al (2011) showed that slight structural modifications of lysozyme are sufficient to greatly improve interfacial properties and foam stability.…”

The effect of formulation variables on protein stability and integrity of a model IgG4 monoclonal antibody and translation to formulation of a model ScFv

“…Monoclonal antibody (mAb) based drugs have been a huge success in the clinic and there are many more in development for the treatment of diseases including cancer and rheumatoid arthritis (Ivanov et al 2009;Ford et al ;Kurata et al;Wang et al 2007;Goi et al ). Although recombinant proteins can be successfully formulated and stabilised by lyophilisation (Smales et al 2002;Povey et al 2009), most of the mAb products currently in the clinic are administered by intravenous infusion (Zhu et al 2014). Due to the 1.5 ml), -400 mg per treatment), this generally means that antibodies must be formulated as high concentration solutions (Dani et al 2007).…”

Interfacial properties, film dynamics and bulk rheology: A multi-scale approach to dairy protein foams

“…For instance, conformational modifications occur in acidic conditions: a molten globule conformation for α-la and a dimerisation by intermolecular β-sheet for β-lg [22,55]. In addition, it has been shown an increase of lysozyme glycation when the pH prior to freeze-drying decrease (pH 6.2, 7.2, or 8.2) [56]. Some authors have suggested that lactosylation of β-lg may be limited by reducing the pH prior to drying [57].…”