In vitro digestibility of β-casein and β-lactoglobulin under simulated human gastric and duodenal conditions: A multi-laboratory evaluation

被引：128

作者：

Mandalari, G. ^{[1
]}

Adel-Patient, K. ^{[2
]}

Barkholt, V. ^{[3
]}

Baro, C. ^{[4
]}

Bennett, L. ^{[5
]}

Bublin, M. ^{[6
]}

Gaier, S. ^{[6
]}

Graser, G. ^{[7
]}

Ladics, G. S. ^{[8
]}

Mierzejewska, D. ^{[9
]}

Vassilopoulou, E. ^{[10
]}

Vissers, Y. M. ^{[11
]}

Zuidmeer, L. ^{[12
]}

Rigby, N. M. ^{[1
]}

Salt, L. J. ^{[1
]}

Defernez, M. ^{[1
]}

Mulholland, F. ^{[1
]}

Mackie, A. R. ^{[1
]}

Wickham, M. S. J. ^{[1
]}

Mills, E. N. C. ^{[1
]}

机构：

[1] Inst Food Res, Norwich NR4 7UA, Norfolk, England

[2] iBiTecS, CEA SPI, Lab Immunoallergie Alimentaire, INRA,UR496, F-91191 Gif Sur Yvette, France

[3] Tech Univ Denmark, Dept Syst Biol, DK-2800 Lyngby, Denmark

[4] ISPA CNR, Turin, Italy

[5] Food Sci Australia, Werribee, Vic 3030, Australia

[6] Med Univ Vienna, Dept Pathophysiol, Ctr Physiol Pathophysiol & Immunol, Vienna, Austria

[7] Syngenta Biotechnol Inc, Res Triangle Pk, NC USA

[8] DuPont Co Inc, Wilmington, DE USA

[9] Polish Acad Sci, Dept Food Chem, Inst Anim Reprod & Food Res, PL-10747 Olsztyn, Poland

[10] Univ Athens, Paediat Clin, Athens, Greece

[11] Wageningen Univ, Food Chem Lab, NL-6700 EV Wageningen, Netherlands

[12] Univ Amsterdam, Acad Med Ctr, NL-1105 AZ Amsterdam, Netherlands

来源：

REGULATORY TOXICOLOGY AND PHARMACOLOGY | 2009年 / 55卷 / 03期

基金：

英国生物技术与生命科学研究理事会;

关键词：

In vitro digestion; beta-Casein; beta-Lactoglobulin; Physiological protocol; Allergy; HUMAN PANCREATIC-JUICE; FOOD ALLERGENS; GASTROINTESTINAL PROTEOLYSIS; PROTEIN DIGESTIBILITY; PEPSIN DIGESTION; STABILITY; FLUID; HYDROLYSIS; RESISTANCE; PH;

D O I：

10.1016/j.yrtph.2009.08.010

中图分类号：

DF [法律]; D9 [法律]; R [医药、卫生];

学科分类号：

0301 ; 10 ;

摘要：

Initially the resistance to digestion of two cow's milk allergens, beta-casein, and beta-lactoglobulin (beta-Lg), was compared using a "high-protease assay" and a "low-protease assay" in a single laboratory. The low-protease assay represents an alternative standardised protocol mimicking conditions found in the gastrointestinal tract. For the high-protease assay, both proteins were incubated with either pepsin or pancreatin and digestion monitored by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse phase-high performance liquid chromatography. The low-protease assay involved gastroduodenal digestion in the presence or absence of phosphatidylcholine (PC). Both beta-casein and beta-Lg were susceptible to hydrolysis by pepsin and pancreatin in the high-protease assay. In contrast, the kinetics of beta-casein digestion in the low-protease assay were slower, beta-Lg being pepsin resistant. During duodenal digestion, beta-Lg was gradually degraded and addition of PC slowed digestion. Subsequently, the reproducibility of the low-protease assay was assessed in 12 independent laboratories by visual assessment of the gels and densitometric analysis: the inter- and intra-laboratory variability was affected by sampling and electrophoresis method employed. The low-protease assay was shown to be reproducible. Future studies will extend these findings using a broader panel of proteins. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：372 / 381

页数：10

共 36 条

[21] CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].