Effects of Disulfide Reduction on the Emulsifying Properties of Bovine Serum Albumin

Lee, Jin Young; Hirose, Masaaki

doi:10.1271/bbb.56.1810

Cited by 12 publications

(1 citation statement)

References 4 publications

(9 reference statements)

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“…Figure shows the SDS-PAGE results, while native PAGE results are presented in the Supporting Information (Figure S6). BSA is known to form aggregates of different sizes under the stress conditions. , The monomer of BSA is a single polypeptide chain protein with molecular weight of ∼66 kDa and is represented as the single most abundant SDS-PAGE band (Figure ). The BSA fraction in both feed and permeate samples is mainly represented by the monomer.…”

Section: Resultsmentioning

confidence: 99%

Protein–Nanocellulose Interactions in Paper Filters for Advanced Separation Applications

2017

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Protein-based pharmaceutics are widely explored for healthcare applications, and 6 out of 10 best-selling drugs today are biologicals. The goal of this work was to evaluate the protein nanocellulose interactions in paper filter for advanced separation applications such as virus removal filtration and bioprocessing. The protein recovery was measured for bovine serum albumin (BSA), γ-globulin, and lysozyme using biuret total protein reagent and polyacrylamide gel electrophoresis (PAGE), and the throughput was characterized in terms of flux values from fixed volume filtrations at various protein concentrations and under worst-case experimental conditions. The affinity of cellulose to bind various proteins, such as BSA, lysozyme, γ-globulin, and human IgG was quantified using a quartz crystal microbalance (QCMB) by developing a new method of fixing the cellulose fibers to the electrode surface without cellulose dissolution-precipitation. It was shown that the mille-feuille filter exhibits high protein recovery, that is, ∼99% for both BSA and lysozyme. However, γ-globulin does not pass through the membrane due to its large size (i.e., >180 kDa). The PAGE data show no substantial change in the amount of dimers and trimers before and after filtration. QCMB analysis suggests a low affinity between the nanocellulose surface and proteins. The nanocellulose-based filter exhibits desirable inertness as a filtering material intended for protein purification.

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Section: Resultsmentioning

confidence: 99%