title: Crosslinking of sodium caseinate by a microbial transglutaminase.
abstract: Sodium caseinate is an effective substrate for transglutaminase. Crosslinking takes place at fast reaction rates resulting in high degrees of crosslinking. The polymers can be hydrolysed by trypsin, but the proteolysates contain residual portions of non- or partlyhydrolysed aggregates. Crosslinking of hydrolysed sodium caseinate decreased the number of free amino groups, but leads only to a very small increase in molecular weight of the peptides.
authors.affiliation: Federal Dairy Research Centre, Kiel, Germany.
authors.forename: P C
authors.initials: PC
authors.lastname: Lorenzen
authors.forename: E
authors.initials: E
authors.lastname: Schlimme
authors.forename: N
authors.initials: N
authors.lastname: Roos
mesh_terms: D002364:Caseins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents; D006868:Hydrolysis; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry; D011503:Transglutaminases / Q000737:chemistry*; D014357:Trypsin
chemical_list: D002364:Caseins; D003432:Cross-Linking Reagents; D010455:Peptides; D011503:Transglutaminases; D014357:Trypsin