2009
DOI: 10.1016/j.foodres.2009.04.022
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Functional properties of milk proteins as affected by enzymatic oligomerisation

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Cited by 67 publications
(54 citation statements)
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References 67 publications
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“…It was also found that treatment of milk proteins by lactoperoxidase led to the formation of protein polymers (Hiller & Lorenzen, 2009 aforementioned three studies provided support to the present study that the ternary system could induce protein cross-linking in the milk. One study reported that the skimmed milk powders treated by TGase at 3-10 U/g protein for 2 h had average degrees of protein polymerization of 23.6-33.9%, respectively (Guyot & Kulozik, 2011).…”
Section: Resultssupporting
confidence: 84%
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“…It was also found that treatment of milk proteins by lactoperoxidase led to the formation of protein polymers (Hiller & Lorenzen, 2009 aforementioned three studies provided support to the present study that the ternary system could induce protein cross-linking in the milk. One study reported that the skimmed milk powders treated by TGase at 3-10 U/g protein for 2 h had average degrees of protein polymerization of 23.6-33.9%, respectively (Guyot & Kulozik, 2011).…”
Section: Resultssupporting
confidence: 84%
“…Transglutaminase (TGase, EC 2.3.2.13) is one of typical enzymes capable of forming isopeptide bonds between the γ-carboxyamide groups and the amino groups and thus can be used to induce cross-linking of food proteins (Beermann & Hartung, 2012;Lorenzen, Neve, Mautner, & Schlimme, 2002) or glycosylation plus cross-linking of casein or soybean proteins (Jiang & Zhao, 2010. The influences of TGase treatment on functional properties of milk proteins had been widely studied (Faegemand & Qvist, 1997;Hiller & Lorenzen, 2009), while the impacts of TGase treatment on the textural and other attributes of yoghurt products were also well characterized (Bönisch, Huss, Weitl, & Kulozik, 2007;Lorenzen et al, 2002). Cross-linking of milk proteins by TGase prior to fermentation could improve gel structure of the set-style yoghurt, resulting in finer protein network with thin strands between the particles (Faegemand & Qvist, 1997;Farnsworth, Li, Hendricks, & Guo, 2006).…”
Section: Introductionmentioning
confidence: 99%
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“…SEC column materials differ in composition and pore volume. The column most frequently used for studying cross-linked casein is Superdex 200, e.g., [30,44,47,48,54,100,115,131,[134][135][136][137][138][139][140][141][142][143][144][145][146][147][148], which is provided by GE Healthcare (Uppsala, Sweden). The column material is based on agarose/dextran with a ratio of pore volume to void volume of V i /V o = 1.7 and exhibits a fractionation range from 10 to 600 kg/mol for globular proteins [128].…”
Section: Separation Principlementioning
confidence: 99%
“…Hiller & Lorenzen applied SEC to compare the efficiency of various enzymes to cross-link different milk protein substrates [131,142], and to assess the susceptibility of sodium caseinate to TGase after dephosphorylation [141].…”
Section: Literature Review Of Studies On Cross-linked Caseinmentioning
confidence: 99%