Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Charles J. Slangen"'
Publikováno v:
International Dairy Journal. 11:363-371
The specificity of the cell-bound, wild-type proteinase (PrtP) of Lactococcus lactis subsp. cremoris SK11 towards the αs1-casein(1–23) fragment under simulated cheese conditions was compared with that of several mutants of PrtP. A unique specifici
Publikováno v:
ResearcherID
Cationic peptides could be successfully released from a precursor protein bound to a cation-exchange membrane by in-situ enzymatic cleavage with an appropriate enzyme. This procedure allows the washing-off of other hydrolytic fragments from the membr
Functionality of β-Casein Peptides: Importance of Amphipathicity for Emulsion-Stabilizing Properties
Autor:
Petra W. J. R. Caessens, Charles J. Slangen, Alphons G. J. Voragen, Harry Gruppen, Servaas Visser
Publikováno v:
Journal of Agricultural and Food Chemistry. 47:1856-1862
To investigate structure-function relationships with regard to emulsion-stabilizing properties, peptides from bovine beta-casein (betaCN), obtained by plasmin hydrolysis and fractionation of the hydrolysate, were isolated and identified on the basis
Publikováno v:
Journal of Chromatography A. 711:141-150
Various components of the beta-casein fraction from bovine milk were separated by preparative reversed-phase high-performance liquid chromatography (RP-HPLC). They included the genetic variants beta A1, beta A2, beta A3, and an unknown component prev
Publikováno v:
Systematic and Applied Microbiology. 18:7-12
Summary The sequence of proteolytic cleavages characterizing the action of chymosin on the αauthor-casein-(24-199)-fragment (αauthor-I) and on β-casein in vitro under conditions as present in Gouda cheese, and the possible intervention by the lact
Publikováno v:
Biochemical Journal. 273:135-139
The specificity of two genetically related cell-envelope serine proteinases (PI-type and PIII-type) of Lactococcus lactis subsp. cremoris towards the alpha s1-casein-(1-23)-fragment, an important intermediate product of primary chymosin-directed prot
Autor:
Charles J. Slangen, Servaas Visser
Publikováno v:
Journal of agricultural and food chemistry. 47(11)
From a bovine whey protein fraction the nonglycosylated and glycosylated alpha-lactalbumin fractions were isolated by gel-permeation chromatography followed by reversed-phase high-performance liquid chromatography. Both fractions were studied by elec
Autor:
Piotr Minkiewicz, Charles J. Slangen, Servaas Visser, Fija M. Lagerwerf, Johan Haverkamp, Harry S. Rollema
Publikováno v:
Journal of chromatography. A. 743(1)
From complex mixtures of non-glycosylated and differently glycosylated caseinomacropeptides (CMP; kappa-casein fragment 106-169; M(r) approximately 7000) various fractions were isolated and further purified by reversed-phase HPLC. The fractions were
Autor:
W. D. van Dongen, Charles J. Slangen, W. Heerma, Arjan J. P. M. Robben, Johan Haverkamp, Servaas Visser
Publikováno v:
Applied microbiology and biotechnology. 41(6)
The specificity of the cell-envelope proteinase (CEPIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine κ-casein was studied. A 4-h digest (pH 6.2, 15°C) of κ-casein was made with the purified proteinase. The pH-4.6 solub
Publikováno v:
Journal of chromatography. 548(1-2)
A reversed-phase high-performance liquid chromatographic method for the separation of the most common and some less common genetic variants of the bovine caseins is described. When the method is used for analysing clarified skim milk, simultaneous id