1993
DOI: 10.1016/0376-7388(93)85150-u
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Fractionation of casein hydrolysates using polysulfone ultrafiltration hollow fiber membranes

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Cited by 26 publications
(17 citation statements)
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“…The molecular mass distribution profile showed higher content of larger peptides (> 2000 Da) in permeates from 10 kDa membranes. These observations are in agreement with previous findings (Pouliot et al, 1993) indicating that the MMCO of polysulfone membranes did not influence to a great extent the separation characteristics of casein hydrolysates.…”
Section: Effect Of Membrane Materials Andmmcosupporting
confidence: 83%
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“…The molecular mass distribution profile showed higher content of larger peptides (> 2000 Da) in permeates from 10 kDa membranes. These observations are in agreement with previous findings (Pouliot et al, 1993) indicating that the MMCO of polysulfone membranes did not influence to a great extent the separation characteristics of casein hydrolysates.…”
Section: Effect Of Membrane Materials Andmmcosupporting
confidence: 83%
“…It can be suggested that by changing the pH of the media from 6.0 to 10.0, the net negative charge of the peptides the pH modifications also induced rneasurable changes in the amino acid profiles in the permeates.ln accordance with previous findings (Pouliot et al, 1993), the UF-fractionation with PS and PES membranes affected the passage of polar amino acids to a greater extent than that of non-polar amino acids. Increasing pH could have affected both basic and acidic amino acids by modifying the ionization of the side chain residues and prornoting peptide-peptide interactions.…”
Section: Effect Of Ph and Edtasupporting
confidence: 77%
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“…Selective isolation of cationic amino acids and peptides by electro-membrane filtration ampholytes (amino acids, peptides and proteins) selectively from complex solutions by manipulating the charge interactions between the components and the membrane surface [4,5,7,9,[16][17][18][19]21]. This can be achieved by adjusting the pH or by adapting the salt composition of the feed.…”
Section: Original Articlementioning
confidence: 99%
“…This approach can be taken further if different proteins are induced to associate with or diffuse from the micelles. For example, Pouliot et al (1993) described dissociation of β-casein from micelles of a phosphocaseinate suspension, which can be microfiltered to produce β-casein-enriched and β-casein-depleted fractions. Mehra and Kelly (2004) demonstrated fractionation of whey proteins into a retentate rich in immunoglobulins, bovine serum albumin and lactoferrin, and a permeate rich in α-lactalbumin and β-lactoglobulin.…”
Section: Fractionation Of Macromoleculesmentioning
confidence: 99%