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Milk Protein Concentration Using Negatively Charged Ultrafiltration Membranes.

ABSTRACT: In this work, milk protein concentrate (MPC) was made using wide-pore negatively charged ultrafiltration membranes. The charged membranes were used for a six-fold volume concentration of skim milk and subsequent diafiltration to mimic the industrial MPC process. The charged 100 kDa membranes had at least a four-fold higher permeate flux at the same protein recovery as unmodified 30 kDa membranes, which are currently used in the dairy industry to make MPC. By placing a negative charge on the surface of an ultrafiltration membrane, the negatively charged proteins were rejected by electrostatic repulsion and not simply size-based sieving. Mass balance models of concentration and diafiltration were developed and the calculations matched the experimental observations. This is the first study to use wide-pore charged tangential-flow membranes for MPC manufacturing. Additionally, a unique mass balance model was applied, which accurately predicted experimental results.

SUBMITTER: Arunkumar A

PROVIDER: S-EPMC6165199 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature

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Milk Protein Concentration Using Negatively Charged Ultrafiltration Membranes.

Arunkumar Abhiram A Etzel Mark R MR

Foods (Basel, Switzerland) 20180828 9

In this work, milk protein concentrate (MPC) was made using wide-pore negatively charged ultrafiltration membranes. The charged membranes were used for a six-fold volume concentration of skim milk and subsequent diafiltration to mimic the industrial MPC process. The charged 100 kDa membranes had at least a four-fold higher permeate flux at the same protein recovery as unmodified 30 kDa membranes, which are currently used in the dairy industry to make MPC. By placing a negative charge on the surf ...[more]

PMID: 30154350

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Project description:The HIV-1 Gag polyprotein precursor composed of the matrix (MA), capsid (CA), nucleocapsid (NC), and p6 domains orchestrates virus assembly via interactions between MA and the cell plasma membrane (PM) on one hand and NC and the genomic RNA on the other hand. As the Gag precursor can adopt a bent conformation, a potential interaction of the NC domain with the PM cannot be excluded during Gag assembly at the PM. To investigate the possible interaction of NC with lipid membranes in the absence of any interference from the other domains of Gag, we quantitatively characterized by fluorescence spectroscopy the binding of the mature NC protein to large unilamellar vesicles (LUVs) used as membrane models. We found that NC, either in its free form or bound to an oligonucleotide, was binding with high affinity (? 10(7) M(-1)) to negatively charged LUVs. The number of NC binding sites, but not the binding constant, was observed to decrease with the percentage of negatively charged lipids in the LUV composition, suggesting that NC and NC/oligonucleotide complexes were able to recruit negatively charged lipids to ensure optimal binding. However, in contrast to MA, NC did not exhibit a preference for phosphatidylinositol-(4,5)-bisphosphate. These results lead us to propose a modified Gag assembly model where the NC domain contributes to the initial binding of the bent form of Gag to the PM.The NC protein is a highly conserved nucleic acid binding protein that plays numerous key roles in HIV-1 replication. While accumulating evidence shows that NC either as a mature protein or as a domain of the Gag precursor also interacts with host proteins, only a few data are available on the possible interaction of NC with lipid membranes. Interestingly, during HIV-1 assembly, the Gag precursor is thought to adopt a bent conformation where the NC domain may interact with the plasma membrane. In this context, we quantitatively characterized the binding of NC, as a free protein or as a complex with nucleic acids, to lipid membranes and showed that the latter constitute a binding platform for NC. Taken together, our data suggest that the NC domain may play a role in the initial binding events of Gag to the plasma membrane during HIV-1 assembly.

Dataset Information

Milk Protein Concentration Using Negatively Charged Ultrafiltration Membranes.

Publications

Milk Protein Concentration Using Negatively Charged Ultrafiltration Membranes.

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