The Citing articles tool gives a list of articles citing the current article.CrossRef Cited-by Linking Program
Cited article:
Alexander Tolkach , Ulrich Kulozik
Lait, 87 4-5 (2007) 301-315
Published online: 2007-10-26
This article has been cited by the following article(s):
135 articles | Pages:
Coupling deterministic and random sequential approaches for structure and texture prediction of a dairy oil-in-water emulsion
Etienne Descamps, Nathalie Perrot, Ioan Cristian Trelea, et al. 25 28 (2014)https://doi.org/10.1016/j.ifset.2013.12.003
Heat-Induced Aggregation of Whey Proteins in Aqueous Solutions below Their Isoelectric Point
Leonardo Cornacchia, Cécile Forquenot de la Fortelle and Paul Venema62 (3) 733 (2014)https://doi.org/10.1021/jf404456q
A CFD model as a tool to simulate β-lactoglobulin heat-induced denaturation and aggregation in a plate heat exchanger
Laurent Bouvier, Anne Moreau, Gilles Ronse, et al. https://doi.org/10.1016/j.jfoodeng.2014.03.025
Formation of β-lactoglobulin aggregates during thermomechanical treatments under controlled shear and temperature conditions
Nicolas Erabit, Denis Flick and Graciela Alvarez120 57 (2014)https://doi.org/10.1016/j.jfoodeng.2013.07.003
Studies on the viability of Saccharomyces boulardii within microcapsules in relation to the thermomechanical properties of whey protein
Diep Duongthingoc, Paul George, Elizabeth Gorczyca and Stefan Kasapis42 232 (2014)https://doi.org/10.1016/j.foodhyd.2013.07.024
A Comparison of the Effectiveness of Sonication, High Shear Mixing and Homogenisation on Improving the Heat Stability of Whey Protein Solutions
Li Ling A. Koh, Jayani Chandrapala, Bogdan Zisu, et al. 7 (2) 556 (2014)https://doi.org/10.1007/s11947-013-1072-1
β-Lactoglobulin films with spiral cracks
Ronald Gebhardt and Ieva Petkeviciute1 (2) 155 (2014)https://doi.org/10.1016/j.foostr.2013.11.003
Stability of Whey Proteins during Thermal Processing: A Review
Heni B. Wijayanti, Nidhi Bansal and Hilton C. Deeth13 (6) 1235 (2014)https://doi.org/10.1111/1541-4337.12105
The use of ultrasonic feed pre-treatment to reduce membrane fouling in whey ultrafiltration
Li Ling A. Koh, Hanh Thi Hong Nguyen, Jayani Chandrapala, et al. 453 230 (2014)https://doi.org/10.1016/j.memsci.2013.11.006
Plasmin activity as a possible cause for age gelation in UHT milk produced by direct steam infusion
Valentin M. Rauh, Anja Sundgren, Mette Bakman, et al. 38 (2) 199 (2014)https://doi.org/10.1016/j.idairyj.2013.12.007
Caseinomacropeptide modifies the heat-induced denaturation–aggregation process of β-lactoglobulin
Thomas Croguennec, Ning Leng, Pascaline Hamon, et al. 36 (1) 55 (2014)https://doi.org/10.1016/j.idairyj.2014.01.004
The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
Raffaele Mezzenga and Peter Fischer76 (4) 046601 (2013)https://doi.org/10.1088/0034-4885/76/4/046601
In-line characterization of a whey protein aggregation process: Aggregates size and rheological measurements
Fatou Toutie Ndoye, Nicolas Erabit, Denis Flick and Graciela Alvarez115 (1) 73 (2013)https://doi.org/10.1016/j.jfoodeng.2012.09.021
Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate
Srinivasan Damodaran and Kingsley K. Agyare30 (1) 12 (2013)https://doi.org/10.1016/j.foodhyd.2012.04.012
Effect of calcium chloride and moderate shear on β-lactoglobulin aggregation in processing-like conditions
Nicolas Erabit, Denis Flick and Graciela Alvarez115 (1) 63 (2013)https://doi.org/10.1016/j.jfoodeng.2012.09.020
Assessing the heat induced changes in major cow and non-cow whey proteins conformation on kinetic and thermodynamic basis
Loredana Dumitraşcu, Ekaterini Moschopoulou, Iuliana Aprodu, et al. 111 (1-3) 129 (2013)https://doi.org/10.1016/j.smallrumres.2012.12.019
β-lactoglobulin denaturation, aggregation, and fouling in a plate heat exchanger: Pilot-scale experiments and dimensional analysis
Jeremy Petit, Thierry Six, Anne Moreau, Gilles Ronse and Guillaume Delaplace101 432 (2013)https://doi.org/10.1016/j.ces.2013.06.045
Physical state, molecular mobility and chemical stability of powdered dairy formulations
Iris Schmitz-Schug, Alessandro Gianfrancesco, Ulrich Kulozik and Petra Foerst53 (1) 268 (2013)https://doi.org/10.1016/j.foodres.2013.05.003
https://doi.org/10.1007/978-1-4614-4714-6_7
https://doi.org/10.1002/9781118634301.ch07
Coupling fluid flow, heat transfer and thermal denaturation-aggregation of beta-lactoglobulin using an Eulerian/Lagrangian approach
Etienne Chantoiseau, Artemio Plana-Fattori, Christophe Doursat and Denis Flick113 (2) 234 (2012)https://doi.org/10.1016/j.jfoodeng.2012.05.043
Pressure dissociation of β-lactoglobulin oligomers near their isoelectric point
Ronald Gebhardt, José Toro-Sierra and Ulrich Kulozik8 (46) 11654 (2012)https://doi.org/10.1039/c2sm26335a
Identification of Milk Origin and Process-Induced Changes in Milk by Stable Isotope Ratio Mass Spectrometry
Matteo Scampicchio, Tanja Mimmo, Calogero Capici, Christian Huck, Nadia Innocente, Stephan Drusch and Stefano Cesco60 (45) 11268 (2012)https://doi.org/10.1021/jf302846j
β-Lactoglobulin as a Molecular Carrier of Linoleate: Characterization and Effects on Intestinal Epithelial Cells in Vitro
Solène Le Maux, Linda Giblin, Thomas Croguennec, Saïd Bouhallab and André Brodkorb60 (37) 9476 (2012)https://doi.org/10.1021/jf3028396
Analysis by Raman spectroscopy of the conformational structure of whey proteins constituting fouling deposits during the processing in a heat exchanger
P. Blanpain-Avet, A. Hédoux, Y. Guinet, et al. 110 (1) 86 (2012)https://doi.org/10.1016/j.jfoodeng.2011.12.005
Toward an integrated modeling of the dairy product transformations, a review of the existing mathematical models
J. Foucquier, E. Chantoiseau, S. Le Feunteun, et al. 27 (1) 1 (2012)https://doi.org/10.1016/j.foodhyd.2011.08.002
Exploring the Denaturation of Whey Proteins upon Application of Moderate Electric Fields: A Kinetic and Thermodynamic Study
Ricardo N. Pereira, José A. Teixeira and António A. Vicente59 (21) 11589 (2011)https://doi.org/10.1021/jf201727s
Influence of calcium on β-lactoglobulin denaturation kinetics: Implications in unfolding and aggregation mechanisms
J. Petit, A.-L. Herbig, A. Moreau and G. Delaplace94 (12) 5794 (2011)https://doi.org/10.3168/jds.2011-4470
β-Lactoglobulin and WPI aggregates: Formation, structure and applications
Taco Nicolai, Michel Britten and Christophe Schmitt25 (8) 1945 (2011)https://doi.org/10.1016/j.foodhyd.2011.02.006
Influence of buffer type and concentration on the peptide composition of trypsin hydrolysates of β-lactoglobulin
Seronei Chelulei Cheison, Elena Leeb, Thomas Letzel and Ulrich Kulozik125 (1) 121 (2011)https://doi.org/10.1016/j.foodchem.2010.08.047
Formation of Non-Native β-Lactoglobulin during Heat-Induced Denaturation
Joseph James Kehoe, Lizhe Wang, Edwin R. Morris and André Brodkorb6 (4) 487 (2011)https://doi.org/10.1007/s11483-011-9230-3
Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of β-lactoglobulin: Analysis by LC–ESI-TOF/MS
Seronei Chelulei Cheison, Meike Schmitt, Elena Leeb, Thomas Letzel and Ulrich Kulozik121 (2) 457 (2010)https://doi.org/10.1016/j.foodchem.2009.12.065
Formation and properties of the whey protein/κ-casein complexes in heated skim milk – A review
Laurence Donato and Fanny Guyomarc'h89 (1) 3 (2009)https://doi.org/10.1051/dst:2008033
Mechanism of formation of stable heat-induced β-lactoglobulin microgels
Laurence Donato, Christophe Schmitt, Lionel Bovetto and Martine Rouvet19 (5) 295 (2009)https://doi.org/10.1016/j.idairyj.2008.11.005
Innovative Einsätze der Membrantrenntechnik in der Lebensmitteltechnologie
U. Kulozik and S. Ripperger80 (8) 1045 (2008)https://doi.org/10.1002/cite.200800093
Pages:
101 to 135 of 135 articles
