2017
DOI: 10.1088/1755-1315/61/1/012143
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Adsorption of bovine serum albumin and urease by biochar

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Cited by 3 publications
(3 citation statements)
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“…In contrast, the N 2 -based specific surface area and total pore volume decreased slightly, possibly because of the adsorption of components from the DMEM. This observation is consistent with the adsorption of bovine serum albumin previously described by Wang et al 16 Nevertheless, because only a relatively small proportion of the total DMEM in the experiment was adsorbed, the sorption of media components cannot explain the observed cytotoxic effects and can have had an only minor effect (if any) on PAH desorption due to pore blockage.…”
Section: Resultssupporting
confidence: 92%
“…In contrast, the N 2 -based specific surface area and total pore volume decreased slightly, possibly because of the adsorption of components from the DMEM. This observation is consistent with the adsorption of bovine serum albumin previously described by Wang et al 16 Nevertheless, because only a relatively small proportion of the total DMEM in the experiment was adsorbed, the sorption of media components cannot explain the observed cytotoxic effects and can have had an only minor effect (if any) on PAH desorption due to pore blockage.…”
Section: Resultssupporting
confidence: 92%
“…The differences in surface coverages combined with the equal amounts of adsorbed proteins indicate that most proteins in the S. pasteurii total protein extract have a higher affinity towards hydrophobic surfaces. In fact, several studies have shown that most proteins have a high affinity towards hydrophobic surfaces, including hydrophilic proteins such as BSA, with increased amounts of adsorbed proteins displayed on surfaces with higher hydrophobicity levels [20][21][22][23][24][25][26]55]. Furthermore, though hydrophobic amino acid residues are mostly ingrained inside the protein's molecular structure, a hydrophobic protein core can become exposed due to structural unfolding upon initial binding via electrostatic interactions.…”
Section: Protein Adsorptionmentioning
confidence: 99%
“…In particular, protein adsorption is highly dependent on the surface chemistries of the protein and the sorbent surface, as well as the presence of other proteins. For example, proteins commonly exhibit high affinity towards hydrophobic surfaces, even if they are hydrophilic in nature [20][21][22][23][24][25][26], but that often leads to protein denaturation and sharp decreases in enzymatic activity [27]. Although soils generally display low levels of hydrophobicity [28,29], hydrophobic soils, defined as having contact angles ≥ 90 • , have been documented worldwide and are especially common in surface soils that often dry out or have been exposed to fires [28,[30][31][32][33][34][35][36].…”
Section: Introductionmentioning
confidence: 99%