Protein aggregation in foam fractionation of bovine serum albumin: Effect of protein concentration

2015 ◽  
Vol 103 ◽  
pp. 234-241 ◽  
Author(s):  
Rui Li ◽  
Nian Fu ◽  
Zhaoliang Wu ◽  
Yanji Wang ◽  
Yanyan Wang
2016 ◽  
Vol 220 ◽  
pp. 33-34 ◽  
Author(s):  
Rui Li ◽  
Zhaoliang Wu ◽  
Yanji Wang ◽  
Linlin Ding ◽  
Yanyan Wang

RSC Advances ◽  
2016 ◽  
Vol 6 (116) ◽  
pp. 115183-115188 ◽  
Author(s):  
Jianlei Liu ◽  
Hao Jing

Glycation with Xyl/Gal could hinder the heat-induced BSA aggregation, and the hindrance effect was enhanced with high glycation degree.


2015 ◽  
Vol 43 ◽  
pp. 228-235 ◽  
Author(s):  
Shuqin Xia ◽  
Yunqi Li ◽  
Qiuyang Xia ◽  
Xiaoming Zhang ◽  
Qingrong Huang

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Yin Hui Chow ◽  
Alagan Sahlini ◽  
Hui-Suan Ng ◽  
John Chi-Wei Lan

AbstractThe efficacy of alcohol/sugar aqueous biphasic (ABS) system on protein extraction was investigated. A model protein, bovine serum albumin (BSA), was adopted to evaluate the effects of types and concentration of phase-forming components, protein concentration, and system pH on the protein partition efficiency. The 1-propanol/maltose ABS exhibited an overall better partition efficiency of BSA to the alcohol-rich top phase. A maximum partition coefficient (K) of 20.01 ± 0.05 and recovery yield (Y) of 95.42% ± 0.01% of BSA were achieved with 35% (w/w) 1-propanol/22% (w/w) maltose ABS at pH 5.0 for 10% (w/w) BSA load. The K and Y of BSA in 1-propanol/maltose ABS was slightly improved with the addition of 3% (w/w) of ionic liquid, 1-butyl-3-methylimidazolium bromide ([Bmim]Br) as the adjuvant that could provide protein stabilizing effect. The Fourier Transform Infrared Spectrum (FTIR) analysis revealed that the protein structure remained unaltered upon the separation process.


OENO One ◽  
2011 ◽  
Vol 45 (1) ◽  
pp. 39
Author(s):  
Belinda S. Kemp ◽  
Roland Harrison ◽  
Richard N. Hider

<p style="text-align: justify;"><strong>Aims</strong>: The main objective of the study was to ascertain whether an existing protein precipitation assay could be simply modified to determine tannin at low concentration in wines. This was achieved by mixing a greater volume of wine to a smaller, but more concentrated, volume of bovine serum albumin (BSA) to maintain the same wine-to-BSA ratio (although both the final pH and ethanol concentration varied). In addition, dilution series of each of these mixtures were prepared to investigate the effect of wine-to-BSA ratio on tannin precipitation.</p><p style="text-align: justify;"><strong>Methods and results</strong>: Seven New Zealand red wines were assayed according to the BSA method using a range of protein (BSA) and wine concentrations achieved by varying wine dilutions and the volume of the model wine solution. Maximum precipitation was observed at lower wine/protein ratios in diluted wines and tannin precipitation increased as protein concentration increased. It was observed that the estimation of tannin concentration in red wine is a product of tannin/protein ratio and BSA concentration. Consequently, the methylcellulose precipitation (MCP) assay was performed to independently determine tannin concentration in red wines. Results indicate that tannin/protein ratio, BSA concentration and possibly tannin composition affect BSA-tannin precipitation.</p><p style="text-align: justify;"><strong>Conclusion</strong>: For the BSA assay there appears to be a region of low tannin/protein ratio within which lower wine tannin concentrations can be determined. Overall it is suggested that tannin precipitation is linearly related to tannin concentration.</p><p style="text-align: justify;"><strong>Significance and impact of the study</strong>: Results showed the limits of the BSA method for low tannin wines and the difficulty in using the method for wines with unknown tannin concentrations.</p>


PLoS ONE ◽  
2017 ◽  
Vol 12 (2) ◽  
pp. e0170869 ◽  
Author(s):  
Marcelo Verdugo ◽  
Jorge Ruiz Encinar ◽  
José Manuel Costa-Fernández ◽  
Mario Menendez-Miranda ◽  
Diego Bouzas-Ramos ◽  
...  

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