Zobrazeno 1 - 7
of 7
pro vyhledávání: '"José Toro-Sierra"'
Publikováno v:
Foods, Vol 7, Iss 7, p 101 (2018)
The use of bioactive bovine milk immunoglobulins (Ig) has been found to be an alternative treatment for certain human gastrointestinal diseases. Some methodologies have been developed with bovine colostrum. These are considered in laboratory scale an
Externí odkaz:
https://doaj.org/article/b2873450af3e4e238a4ff957ed7bb602
Publikováno v:
Dairy Science & Technology. 93:487-503
The particle size of microparticulated whey proteins is decisive for the sensory properties and applicability of these products in foodstuffs. The impact of spray-drying conditions on the particle size of whey microparticles was studied. Solutions of
Publikováno v:
Food and Bioprocess Technology. 6:1032-1043
An optimized fractionation method in the pilot scale for production of isolated α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) was developed. The method comprises following steps: (1) selective thermal precipitation of α-La, (2) aging of the fo
Publikováno v:
International Dairy Journal. 21:166-171
Whey protein isolate (93.84% protein) was hydrolysed using bovine trypsin (EC 3.4.21.4) at an enzyme-to-substrate ratio of 1.0% (w w −1 ) over a range of temperatures and pH. Residual protein was quantified using reversed-phase high performance liq
Publikováno v:
Foods
Volume 7
Issue 7
Foods, Vol 7, Iss 7, p 101 (2018)
Volume 7
Issue 7
Foods, Vol 7, Iss 7, p 101 (2018)
The use of bioactive bovine milk immunoglobulins (Ig) has been found to be an alternative treatment for certain human gastrointestinal diseases. Some methodologies have been developed with bovine colostrum. These are considered in laboratory scale an
The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e5540d19c2c4e5fe86cb0c93f2a5785
https://doi.org/10.1017/s0022029912000416
https://doi.org/10.1017/s0022029912000416
Publikováno v:
Soft Matter. 8:11654
We study pressure dissociation of aggregated states of β-lactoglobulin at pH 4.6 using static and dynamic light scattering. We find that octamers dissociate at 20 °C into dimers at pressures P 180 MPa.