1998
DOI: 10.1002/(sici)1097-0290(19980105)57:1<109::aid-bit13>3.0.co;2-f
|View full text |Cite
|
Sign up to set email alerts
|

Ionic interactions in nanofiltration of β casein peptides

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
26
0

Year Published

2006
2006
2015
2015

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 35 publications
(28 citation statements)
references
References 26 publications
2
26
0
Order By: Relevance
“…According Speroni et al (2010), during the processing of tofu the isoflavones may be involved in different kinds of interactions with proteins because of their diverse polarity and hydrophobicity characteristics, as well as their ability to form hydrogen bonds. On the other hand, Garem et al (1998) noted that the presence of high molar mass compounds, such as proteins and …”
Section: Nanofiltration (Nf) Processmentioning
confidence: 99%
“…According Speroni et al (2010), during the processing of tofu the isoflavones may be involved in different kinds of interactions with proteins because of their diverse polarity and hydrophobicity characteristics, as well as their ability to form hydrogen bonds. On the other hand, Garem et al (1998) noted that the presence of high molar mass compounds, such as proteins and …”
Section: Nanofiltration (Nf) Processmentioning
confidence: 99%
“…Membrane separation using tight ultrafiltration (UF) and nanofiltration (NF) approaches have been used to fractionate protein hydrolysates (Garem et al, 1998;Pouliot et al, 1999;Groleau et al, 2004;Lapointe et al, 2005). Publications on this area highlight the important role of membrane-peptide electrostatic interactions in the differential separation of peptides with similar molecular weight (MW) but with different net charge.…”
Section: Introductionmentioning
confidence: 99%
“…Another subsequent work reported the interesting potential of NF membranes for separating peptides in the range of 0.3-1 kDa [68]. Specific conditions of ionic strength and especially pH promoted the separation of peptides because the membrane and peptides showed amphoteric properties.…”
Section: Nf Applied To Amino Acid and Peptide Fractionation: Reviewmentioning
confidence: 98%
“…Several authors have demonstrated the preponderance of a selectivity based on electrostatic interactions at low ionic strength values [16,68,85]. The fact that electrostatic interactions membrane-peptide lose significance at high ionic strength values results in a decrease of the double selectivity size/charge in processes involving NF membranes.…”
Section: Main Parameters Influencing Peptide Fractionation Using Nf Mmentioning
confidence: 99%
See 1 more Smart Citation