The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

Kehoe, Joseph J.; Morris, Edwin R.; Brodkorb, André

doi:10.1016/j.foodhyd.2006.10.001

Cited by 19 publications

(16 citation statements)

References 23 publications

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“…Comparing the results of Figure 5 with results of previous authors who published similar chromatograms (Outinen et al. 1996; Cheang and Zydney 2003; Kehoe et al. 2007), we can deduce that peaks 1 and 2 probably correspond to β‐Lg in the form of dimer and monomer, respectively, and peak 3 to α‐La.…”

Section: Resultssupporting

confidence: 71%

An investigation of the fractionation of whey proteins by two microfiltration membranes with nominal pore size of 0.1 μm

Baldasso

Kanan

Tessaro

2011

Int J of Dairy Tech

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There is growing interest in the fractionation of whey proteins because of the specific properties of individual whey proteins. The objective of this work was to assess the efficiency of two membranes to obtain two fractions, one rich in β‐lactoglobulin (β‐Lg) and the other rich in α‐lactalbumin (α‐La) from a whey‐protein concentrate using microfiltration (MF). Two MF membranes were tested for the fractionation: a flat‐sheet membrane VCWP and a spiral membrane MF‐7002, both with nominal pore sizes of 0.1 μm. The VCWP retained 78% of the proteins in solution, and this membrane was shown to be permeable to both proteins, β‐Lg and α‐La. The retention of protein by MF‐7002 was 65%, and there was a partial retention of lactose. The permeate collected in the MF‐7002 in the concentration stage was over 50%α‐La; although this was present in lower concentrations, it was passed preferentially to the permeate. The results indicated that some aggregation of the proteins may have occurred under the experimental conditions because there was only a partial separation of the proteins under study.

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Section: Resultssupporting

confidence: 71%

An investigation of the fractionation of whey proteins by two microfiltration membranes with nominal pore size of 0.1 μm

Baldasso

Kanan

Tessaro

2011

Int J of Dairy Tech

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“…Gelatin (up to 1%) was effective in a concentrationdependent manner in inhibiting heat -induced aggregation of LMW -UK. 149,211 In contrast, replacing β -lactoglobulin with increasing amounts of BSA while keeping the total protein concentration constant at 5% (w/w) signifi cantly increased the denaturation (and aggregation) rate of β -lactoglobulin at 78 ° C. 212 Results clearly indicate that BSA contributed to the formation of intermolecular disulfi de bonds in heat -induced denaturation/aggregation. Similarly, BSA at 30 mg/mL was shown to accelerate fi brillation of S -carboxymethyl -α -lactalbumin during stirring at 37 ° C. 163 Some proteins inhibit/prevent aggregation of other proteins, likely through chaperone -like activities.…”

Section: Amphoteric Polymers/proteinsmentioning

confidence: 96%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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“…Consequently, several studies exist on the heat gelation of mixtures of b-lg and a-la or BSA (Hines & Foegeding, 1993;Kavanagh, Clark, Gosal, & Ross-Murphy, 2000;Kehoe, Morris, & Brodkorb, 2007).…”

Section: Introductionmentioning

confidence: 99%

The dynamics of heat gelation of casein glycomacropeptide – β-lactoglobulin mixtures as affected by interactions in the aqueous phase

Martínez

Farı́as

Pilosof

2010

International Dairy Journal

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The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

Cited by 19 publications

References 23 publications

An investigation of the fractionation of whey proteins by two microfiltration membranes with nominal pore size of 0.1 μm

An investigation of the fractionation of whey proteins by two microfiltration membranes with nominal pore size of 0.1 μm

External Factors Affecting Protein Aggregation

The dynamics of heat gelation of casein glycomacropeptide – β-lactoglobulin mixtures as affected by interactions in the aqueous phase

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