Title Asymmetric flow field flow fractionation for the investigation of caseins cross-linked by microbial transglutaminase
Date 28.03.2019
Number 56506
Abstract The cross-linking of caseins with microbial transglutaminase (mTGase) was investigated using asymmetric flow field flow fractionation in combination with static and dynamic light scattering detections (AF4-MALS-DLS). This approach allows determining molar mass, molecular size, scaling properties, and apparent densities of casein aggregates prior to and after enzymatic treatment. The results show that, as a consequence of non-covalent interactions, casein molecules associate to form elongated aggregates with a molar mass () ranging from approx. 4·×·105 to 1.2·×·106·g·mol-1, and a mean radius of gyration () of approx. 16·nm. Upon enzymatic treatment with mTGase, casein aggregates become more compact as increases but decreases with ongoing cross-linking reaction. In contrast, the hydrodynamic radius distribution determined by online DLS is rather unaffected by enzymatic cross-linking, indicating that mTGase cross-links casein molecules mainly within distinct aggregates. Furthermore, extensive enzymatic treatments with mTGase change the molecular shapes of casein aggregates towards more compact and denser spherical structures.
Publisher Food Hydrocolloids
Citation Food Hydrocolloids 92 (2019) 117-124
Authors Abbate, R. A. ; Raak, N. ; Boye, S. ; Janke, A. ; Rohm, H. ; Jaros, D. ; Lederer, A.
Tags casein cross-linking microbial transglutaminase asymmetric flow field flow fractionation light scattering scaling properties

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