Literature DB >> 12797759

A new multistep Ca2+-induced cold gelation process for beta-lactoglobulin.

Cecile Veerman1, Harry Baptist, Leonard M C Sagis, Erik van der Linden.   

Abstract

The objective of this study was to obtain beta-lactoglobulin (beta-lg) gels at very low protein concentrations using a new multistep Ca(2+)-induced cold gelation process. In the conventional cold gelation process, salt free beta-lg solutions were heated at neutral pH, cooled, and cross-linked by adding salts. In our new process, first, long linear beta-lg fibrils were formed at pH 2. Solutions of these fibrils were cooled, and subsequently, the pH was adjusted to 7 or 8. Transmission electron microscopy studies showed that the long linear fibrils formed at pH 2 were stable when the pH was adjusted to 7 or 8. In the final step, the fibrils were cross-linked using CaCl(2). Using rheological measurements, the critical percolation concentration was determined. In the new multistep cold gelation process, the critical percolation concentration was an order of magnitude lower than in the conventional cold gelation method.

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Year:  2003        PMID: 12797759     DOI: 10.1021/jf0261396

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  2 in total

1.  Electric birefringence study of an amyloid fibril system: the short end of the length distribution.

Authors:  S S Rogers; P Venema; J P M van der Ploeg; L M C Sagis; A M Donald; E van der Linden
Journal:  Eur Phys J E Soft Matter       Date:  2005-10-14       Impact factor: 1.890

2.  Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation.

Authors:  Maximilian J Uttinger; Timon R Heyn; Uwe Jandt; Simon E Wawra; Bettina Winzer; Julia K Keppler; Wolfgang Peukert
Journal:  Eur Biophys J       Date:  2020-01-31       Impact factor: 1.733

  2 in total

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