Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of β-casein and β-lactoglobulin: A model study with glyoxal, methylglyoxal and butanedione

2017 ◽  
Vol 102 ◽  
pp. 313-322 ◽  
Author(s):  
Di Zhao ◽  
Thao T. Le ◽  
Lotte Bach Larsen ◽  
Lin Li ◽  
Dan Qin ◽  
...  
Keyword(s):  
In Vitro Digestibility ◽  
Dicarbonyl Compounds ◽  
Model Study ◽  
Β Lactoglobulin

scholarly journals Interplay between Residual Protease Activity in Commercial Lactases and the Subsequent Digestibility of β-Casein in a Model System

Molecules ◽  
2019 ◽  
Vol 24 (16) ◽  
pp. 2876 ◽  
Author(s):  
Di Zhao ◽  
Thao T. Le ◽  
Lotte Bach Larsen ◽  
Yingqun Nian ◽  
Cong Wang ◽  
...  
Keyword(s):  
Milk Proteins ◽  
Model System ◽  
In Vitro Digestibility ◽  
Lactose Hydrolysis ◽  
Hydrolysis Method ◽  
Model Study ◽  
C Terminus ◽  
Heat Treated ◽  
Peptide Profiles

One of the conventional ways to produce lactose-hydrolyzed (LH) milk is via the addition of commercial lactases into heat-treated milk in which lactose is hydrolyzed throughout storage. This post-hydrolysis method can induce proteolysis in milk proteins due to protease impurities remaining in commercial lactase preparations. In this work, the interplay between lactose hydrolysis, proteolysis, and glycation was studied in a model system of purified β-casein (β-CN), lactose, and lactases using peptidomic methods. With a lactase presence, the proteolysis of β-CN was found to be increased during storage. The protease side-activities mainly acted on the hydrophobic C-terminus of β-CN at Ala, Pro, Ile, Phe, Leu, Lys, Gln, and Tyr positions, resulting in the formation of peptides, some of which were N-terminal glycated or potentially bitter. The proteolysis in β-CN incubated with a lactase was shown to act as a kind of “pre-digestion”, thus increasing the subsequent in vitro digestibility of β-CN and drastically changing the peptide profiles of the in vitro digests. This model study provides a better understanding of how the residual proteases in commercial lactase preparations affect the quality and nutritional aspects of β-CN itself and could be related to its behavior in LH milk.

Heat‐induced amyloid‐like aggregation of β‐lactoglobulin affected by glycation by α‐dicarbonyl compounds in a model study

2019 ◽  
Vol 100 (2) ◽  
pp. 607-613 ◽  
Author(s):  
Di Zhao ◽  
Xia Zhang ◽  
Dan Xu ◽  
Guoying Su ◽  
Bing Li ◽  
...  
Keyword(s):  
Dicarbonyl Compounds ◽  
Model Study ◽  
Β Lactoglobulin

In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin

2006 ◽  
Vol 16 (4) ◽  
pp. 294-302 ◽  
Author(s):  
Samira Roufik ◽  
Sylvie F. Gauthier ◽  
Sylvie L. Turgeon
Keyword(s):  
Bioactive Peptides ◽  
In Vitro Digestibility ◽  
Β Lactoglobulin

scholarly journals Effects of Different Levels of Gum Arabic, Low Methylated Pectin and Xylan on In Vitro Digestibility of β-Lactoglobulin

2003 ◽  
Vol 86 (12) ◽  
pp. 3857-3865 ◽  
Author(s):  
J. Mouécoucou ◽  
C. Sanchez ◽  
C. Villaume ◽  
O. Marrion ◽  
S. Frémont ◽  
...  
Keyword(s):  
Gum Arabic ◽  
In Vitro Digestibility ◽  
Β Lactoglobulin ◽  
Different Levels
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