Searched for: subject:"Protein%5C%2BBinding"
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Smit, E. (author), Oling, F. (author), Demel, R. (author), Martinez, B. (author), Pouwels, P.H. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
Lactobacillus acidophilus, like many other bacteria, harbors a surface layer consisting of a protein (SA-protein) of 43 kDa. SA-protein could be readily extracted and crystallized in vitro into large crystalline patches on lipid monolayers with a net negative charge but not on lipids with a net neutral charge. Reconstruction of the S-layer from...
article 2001
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Smit, E. (author), Jager, D. (author), Martinez, B. (author), Tielen, F.J. (author), Pouwels, P.H. (author), Centraal Instituut voor Voedingsonderzoek TNO (author)
The structure of the crystallisation domain, SAN, of the S A-protein of Lactobacillus acidophilus ATCC 4356 was analysed by insertion and deletion mutagenesis, and by proteolytic treatment. Mutant S A-protein synthesised in Escherichia coli with 7-13 amino acid insertions near the N terminus or within regions of sequence variation in SAN (amino...
article 2002
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Nieuwenhuizen, W.F. (author), Dekker, H.L. (author), Gröneveld, T. (author), de Koster, C.G. (author), de Jong, G.A.H. (author), TNO Voeding (author)
Bovine β-lactoglobulin (BLG) is a major component in whey and its physical properties are important for the texture of many dairy-based foods. Modification of proteins with transglutaminase from Streptoverticillium mobaraense (MTGase) can be used to alter their physical properties. MTGase-mediated modification of native BLG was until now,...
article 2004