Conjugation of Bovine Serum Albumin and Glucose under Combined High Pressure and Heat

Abstract

The effect of combined heat and pressure on the Maillard reaction between bovine serum albumin (BSA) and glucose was investigated. The effects in the range of 60-132 °C and at 0.1-600 MPa on the lysine availability of BSA were investigated at isothermal/isobaric conditions. The kinetic results showed that the protein-sugar conjugation rate increased with increasing temperature, whereas it decreased with increasing pressure. The reaction followed 1.4th order kinetics at most conditions investigated. A mathematical model describing BSA-glucose conjugation kinetics as a function of pressure and temperature is proposed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and matrix-assisted laser desorption/ionization time-offlight mass spectrometry were used to verify BSA-glucose conjugation and to identify the glucosylated sites. These indicated that the application of combined high pressure and high temperature resulted in significant differences in the progression of the Maillard reaction as compared to heat treatments at atmospheric pressure.

Glycated albumin: an overview of the In Vitro models of an In Vivo potential disease marker

“…This final section intends to introduce in vitro models of albumin glycation, as a mean to study this phenomenon under controlled conditions. The significant impact of glycation on the protein structure could be observed more conveniently by in vitro techniques such as the use of heat and pressure [108]. HSA has approximately 58 lysine residues [80].…”

Isolation and characterization of serum albumin from Camelus dromedarius

“…Serum albumins are multifunctional and economically viable due to their extensive use in the pharmaceutical and biotechnological industries (26,27). They are employed as stabilizers in therapeutic proteins, vaccines and enzymes (28–30). Serum albumins are amphiphilic in nature and could be utilized to prevent adsorption of other active proteins on the surface of the container, or could be included in the formulation to suppress protein aggregation (31,32).…”

Exploring novel food proteins and processing technologies : a case study on quinoa protein and high pressure –high temperature processing

“…Separately, they are known to have a similar effect on whey proteins: they denature and unfold whey proteins, leading to protein aggregation [6]. Together, pressure and heat were shown to increase, reduce or not affect protein aggregation compared to heat alone, as reported by Buckow et al (2011) and in Chapter 5. Similarly, the combination of heat and pressure affected MR differently in several studies.…”

“…Buckow et al (2011) found that protein (BSA) -sugar (glucose) conjugation decreased with increasing pressure during HPHT treatments (0.1-600 MPa, 110°C, 0-50 min, pH 9). They also studied protein unfolding and aggregation.…”

“…It has been reported that pressure has a synergistic effect with heat on whey protein denaturation and unfolding [23,24,9]. Buckow et al (2011) reported that pressures of 600 MPa for up to 45 min at 70°C did not lead to significant unfolding of BSA. However, at higher temperatures, protein unfolding was accelerated, possibly exposing more lysine groups.…”