Modifying Food Texture 2015
DOI: 10.1016/b978-1-78242-333-1.00004-8
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Enzymatic modification of dairy product texture

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Cited by 12 publications
(9 citation statements)
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“…According to Noeparvar and Morison [ 64 ], κ-casein may be related to lactose content given the role of this casein in the stabilization of calcium phosphate of milk, which is the main stabilizing agent of casein micelles [ 65 ]. Furthermore, κ-casein is the only casein that can post-translationally glycosylate via O-linked glycosylation of threonine residues [ 66 ].…”
Section: Discussionmentioning
confidence: 99%
“…According to Noeparvar and Morison [ 64 ], κ-casein may be related to lactose content given the role of this casein in the stabilization of calcium phosphate of milk, which is the main stabilizing agent of casein micelles [ 65 ]. Furthermore, κ-casein is the only casein that can post-translationally glycosylate via O-linked glycosylation of threonine residues [ 66 ].…”
Section: Discussionmentioning
confidence: 99%
“…PPO is a copper‐containing enzyme, which catalyzes the hydroxylation of monophenols to diphenols and oxidation of diphenol to quinone. Further polymerization of quinone will then occur and form brown pigments on food, which is known as the undesirable browning effect (Ercili‐Cura, Huppertz, & Kelly, ). Mechanical damage of food leads to food browning as this reaction can only happen when substrates in the vacuoles mix with enzymes that are located in the chloroplast, in the presence of oxygen (Ioannou & Ghoul, ).…”
Section: Introductionmentioning
confidence: 99%
“…pigments on food, which is known as the undesirable browning effect (Ercili-Cura, Huppertz, & Kelly, 2015). Mechanical damage of food leads to food browning as this reaction can only happen when substrates in the vacuoles mix with enzymes that are located in the chloroplast, in the presence of oxygen (Ioannou & Ghoul, 2013).…”
mentioning
confidence: 99%
“…Microbial tyrosinase was shown to have an ability to oxidise tyrosine at any position of a tripeptide, that is at the N‐terminal, C‐terminal or the middle position (Isaschar‐Ovdat & Fishman, ). The quinones formed, being highly reactive species, can undergo non‐enzymatic reactions with tyrosines, lysines, cysteines or histidines in the same or a different molecule (Flander et al , ; Ercili‐Cura et al , ). In this study, the quinones formed dimers as expected.…”
Section: Resultsmentioning
confidence: 99%