Regulation of protein multipoint adsorption on ion-exchange adsorbent and its application to the purification of macromolecules

Huang, Yongdong; Bi, Jingxiu; Zhao, Lan; Ma, Guanghui; Su, Zhiguo

doi:10.1016/j.pep.2010.07.002

Cited by 29 publications

(16 citation statements)

References 28 publications

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“…The rate is higher than that of previous works that hepatitis B surface antigen (HBsAg) recovered from diethylaminoethyl (DEAE) Sepharose or organic ion-exchange adsorbent showed 66% retention [37]. When ion exchangeable carriers were used as adsorbents for proteins, loss of the biological activity has been often observed [37,38]. This loss of the biological activity could be attributable to the destruction of the protein structure by the multipoint adsorption on ion exchange adsorbents, as the multipoint adsorption can cause some strain in the protein structure.…”

Section: Enzymatic Activity Of Ctra Recovered From K-ltlcontrasting

confidence: 57%

“…CTRA recovered from K-LTL showed efficient enzymatic activity (81 units/mg) that it retains approximately 84% of the initial activity. The rate is higher than that of previous works that hepatitis B surface antigen (HBsAg) recovered from diethylaminoethyl (DEAE) Sepharose or organic ion-exchange adsorbent showed 66% retention [37]. When ion exchangeable carriers were used as adsorbents for proteins, loss of the biological activity has been often observed [37,38].…”

Section: Enzymatic Activity Of Ctra Recovered From K-ltlmentioning

confidence: 75%

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Adsorption and desorption behavior of basic proteins on zeolites

Matsui

Kiyozumi

Mizushina

et al. 2015

Separation and Purification Technology

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Section: Enzymatic Activity Of Ctra Recovered From K-ltlcontrasting

confidence: 57%

Section: Enzymatic Activity Of Ctra Recovered From K-ltlmentioning

confidence: 75%

Adsorption and desorption behavior of basic proteins on zeolites

Matsui

Kiyozumi

Mizushina

et al. 2015

Separation and Purification Technology

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“…It was compared to

q_{m}

for human serum albumin on DEAE‐Spherodex and DEAE‐Sepharose FF . Considering the specific surface area of the adsorbent (∼30 m 2 /mL) , this value was less than the limiting value of the two‐dimensional protein binding capacity (∼2.0 mmol/L)[ . Thus, it was convinced that both proteins were adsorbed in a monolayer on Q Sepharose FF.…”

Section: Resultsmentioning

confidence: 99%

Single and binary adsorption of proteins on ion‐exchange adsorbent: The effectiveness of isothermal models

Liang

Fieg

Shi

et al. 2012

J of Separation Science

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Simultaneous and sequential adsorption equilibria of single and binary adsorption of bovine serum albumin and bovine hemoglobin on Q Sepharose FF were investigated in different buffer constituents and initial conditions. The results in simultaneous adsorption showed that both proteins underwent competitive adsorption onto the adsorbent following greatly by protein-surface interaction. Preferentially adsorbed albumin complied with the universal rule of ion-exchange adsorption whereas buffer had no marked influence on hemoglobin adsorption. Moreover, an increase in initial ratios of proteins was benefit to a growth of adsorption density. In sequential adsorption, hemoglobin had the same adsorption densities as single-component adsorption. It was attributed to the displacement of preadsorbed albumin and multiple layer adsorption of hemoglobin. Three isothermal models (i.e. extended Langmuir, steric mass-action, and statistical thermodynamic (ST) models) were introduced to describe the ion-exchange adsorption of albumin and hemoglobin mixtures. The results suggested that extended Langmuir model gave the lowest deviation in describing preferential adsorption of albumin at a given salt concentration while steric mass-action model could very well describe the salt effect in albumin adsorption. For weaker adsorbed hemoglobin, ST model was the preferred choice. In concert with breakthrough data, the research further revealed the complexity in ion-exchange adsorption of proteins.

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“…Several works have been conducted with the purpose of recovering and purifying whey proteins by different methods [8][9][10][11][12][13]. Ion-exchange chromatography (IEC) has been extensively employed in protein recovery and purification [14][15][16][17][18][19]. IEC is advantageous because separation typically occurs in the presence of aqueous buffers and hydrophilic surfaces as opposed to the harsher solvents and hydrophobic stationary phases used in reversed-phase chromatography.…”

Section: Introductionmentioning

confidence: 99%