2020
DOI: 10.1016/j.jchromb.2020.122435
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Amino acid-based hydrophobic affinity cryogel for protein purification from ora-pro-nobis (Pereskia aculeata Miller) leaves

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Cited by 10 publications
(3 citation statements)
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“…The swelling capacity was characterized as the amount of water absorbed by the dry cryogel and the degree of expansion by the difference between the mass of the dehydrated and hydrated cryogel, presenting the values of 11.4 ± 0.5 g/g and 16.26 ± 0.3 mL/g, respectively. These analyses show that the cryogel mass occupies a large volume when hydrated, reinforcing the nature of its porous structure, as well as a sponge and elastic characteristic and consistent, confirming what has been reported for other types of activated cryogels [29‐30, 21, 31].…”
Section: Resultssupporting
confidence: 86%
See 1 more Smart Citation
“…The swelling capacity was characterized as the amount of water absorbed by the dry cryogel and the degree of expansion by the difference between the mass of the dehydrated and hydrated cryogel, presenting the values of 11.4 ± 0.5 g/g and 16.26 ± 0.3 mL/g, respectively. These analyses show that the cryogel mass occupies a large volume when hydrated, reinforcing the nature of its porous structure, as well as a sponge and elastic characteristic and consistent, confirming what has been reported for other types of activated cryogels [29‐30, 21, 31].…”
Section: Resultssupporting
confidence: 86%
“…These low and constant values along flow velocities indicate that the mass transfer region is small, and the mass transfer occur predominantly by convection. This behavior is like the studies reported by Mól et al [21] and Neves et al [30]. The experimental pressure drop as a function of different flow velocities are shown in Figure 6.…”
Section: Characterization Of the Affinity Columnsupporting
confidence: 88%
“…At the same time, the high-pressure and enzymatic hydrolysis treatments may also increase hydrophobic amino acid content in gelatin peptides, thereby improving their stability and antioxidant properties. Studies have also indicated that proteins with a high content of hydrophobic amino acids exhibit greater stability ( Cristina Oliveira Neves, Aparecida Rodrigues, Teixeira Valentim, Cristina Freitas de Oliveira Meira, Henrique Silva, Ayra Alcântara Veríssimo, et al, 2020 ).…”
Section: Resultsmentioning
confidence: 99%