Whey protein membrane processing methods and membrane fouling mechanism analysis

Wang, Wen-Qiong; Wa, Yunchao; Xiao-feng, Zhang; Gu, Ruixia; Mao-lin, LU

doi:10.1016/j.foodchem.2019.03.086

Cited by 81 publications

(39 citation statements)

References 128 publications

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“…Whey was originally considered as the soluble serum proteins that remain after precipitation of casein during cheese production. Other methods to gain whey proteins are based on ion exchangers [36] and membrane filtration [37]. TGF-β is heat stable and resists low pH, they are both conditions that can even increase the activity of the preforms of the growth factor [23].…”

Section: Discussionmentioning

confidence: 99%

Micellar Casein and Whey Powder Hold a TGF-β Activity and Regulate ID Genes In Vitro

et al. 2021

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Casein and whey being food supplements have been considered to be used in oral health care products. However, the response of oral cells to micellar casein and whey powder remains unclear. Considering that milk contains the growth factor TGF-β, and lactoperoxidase was recently reported to decrease the expression of inhibitor of DNA-binding (ID) proteins, there is a rationale to assume that casein and whey can also provoke these responses in oral cells. To examine the TGF-β activity, gingival fibroblasts were exposed to reconstituted casein and whey powder from food supplement before the expression of TGF-β target genes were analyzed by reverse transcription-quantitative polymerase chain reaction. Immunoassays were performed for interleukin11 (IL11) in the cell culture supernatant and for TGF-β in the reconstituted casein and whey. We blocked TGF-β by neutralizing the antibody and the TGF-β receptor type I kinase with the inhibitor SB431542. We also showed smad3 phosphorylation and smad2/3 nuclear translocation by Western blot and immunostaining, respectively. Moreover, with reconstituted casein and whey powder, ID1 and ID3 expression analysis was evaluated in HSC2 human oral squamous carcinoma cells. We report here that casein and whey powder caused a robust increase of TGF-β target genes interleukin11 (IL11), NADPH oxidase 4 (NOX4) and proteoglycan4 (PRG4) in gingival fibroblasts that was blocked by SB431542 and the neutralizing antibody. Moreover, casein and whey powder increased the phosphorylation of smad3 and nuclear translocation of smad2/3. No changes of proliferation markers Ki67 and cyclinD1 were observed. Furthermore, reconstituted casein and whey powder decreased ID1 and ID3 expression in the HSC2 oral squamous carcinoma cells. These findings suggest that the processing of milk into casein and whey powder maintains the TGF-β activity and its capacity to regulate ID1 and ID3 genes in oral fibroblasts and oral squamous carcinoma cells, respectively. These data increase the scientific knowledge on the biological activity of casein and whey with a special emphasis on oral health.

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Section: Discussionmentioning

confidence: 99%

Micellar Casein and Whey Powder Hold a TGF-β Activity and Regulate ID Genes In Vitro

et al. 2021

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“…In the last two decades, the application and processing of proteins in food, biological, pharmaceutical and chemistry industries have increased due to their use as food supplement (i.e. whey protein) 1 , 2 , hormones, vaccines, antibiotics, antibodies and biopharmaceutical enzymes 3 , among others. Obtaining high quality proteins for delivery to the final consumers is a major concern of the industries and, for this reason, the processing of proteins is necessary.…”

Section: Introductionmentioning

confidence: 99%

Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme

Miron

Espindola

Dutournié

et al. 2021

Sci Rep

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During the processing of biomolecules by ultrafiltration, the lysozyme enzyme undergoes conformational changes, which can affect its antibacterial activity. Operational conditions are considered to be one of the main parameters responsible for such changes, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can result in different properties of the protein after filtration, due to their different pore network. The filtration of lysozyme, regardless of the membrane, produces a decrease in the membrane hydraulic permeability (between 10 and 30%) and an increase in its selectivity in terms of observed rejection rate (30%). For the filtrated lysozyme, it appears that the HPLC retention time increases depending on the membrane used. The antibacterial activity of the filtrated samples is lower than the native protein and decreases with the increase of the applied pressure reaching 55–60% loss for 12 bar which has not been reported in the literature before. The observed results by SEC-HPLC and bacteriological tests, suggest that the conformation of the filtrated molecules are indeed modified. These results highlight the relationship between protein conformation or activity and the imposed shear stress.

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“…In the last two decades, the application and processing of proteins in food, biological, pharmaceutical and chemistry industries have been increased due to their applications such as food supplement (whey protein) [1,2], as hormones, vaccines, antibiotics, antibodies and enzymes in biopharmaceutical [3], among others. Obtaining high quality proteins to delivery to the nal consumers is a major concern of the industries and, for this, processing them is necessary.…”

Section: Introductionmentioning

confidence: 99%

Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme

Miron

Espindola

Dutournié

et al. 2021

Preprint

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During the processing of biomolecules by ultrafiltration, the lysozyme enzyme suffers conformational changes, which can affect its antibacterial activity. Operational conditions are considered ones of the principal responsible for the modifications, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can produce different properties on the protein after filtration, due to their different pore network. The filtration of lysozyme, regardless of the membrane, produces a decrease in the membrane hydraulic permeability (between 10–30%) and an increase in its selectivity in terms of observed rejection rate (30%). For the filtrated lysozyme, it appears that the HPLC retention time increases depending on the membrane used. The antibacterial activity of the filtrated samples is lower than the native protein and decreases with the increase of the applied pressure reaching 55–60% loss for 12 bar which is not reported in the literature. The observed results by SEC-HPLC and bacteriological tests, suggest that the conformation of the filtrated molecules are indeed modified. These results highlight the relationship between protein conformation or activity and the imposed shear stress.

show abstract

Whey protein membrane processing methods and membrane fouling mechanism analysis

Cited by 81 publications

References 128 publications

Micellar Casein and Whey Powder Hold a TGF-β Activity and Regulate ID Genes In Vitro

Micellar Casein and Whey Powder Hold a TGF-β Activity and Regulate ID Genes In Vitro

Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme

Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme

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