Impacts of glycation and transglutaminase-catalyzed glycosylation with glucosamine on the conformational structure and allergenicity of bovine β-lactoglobulin-Reference-Cited by-同舟云学术

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Impacts of glycation and transglutaminase-catalyzed glycosylation with glucosamine on the conformational structure and allergenicity of bovine β-lactoglobulin

Published:2018 Issue:7 Volume:9 Page:3944-3955
ISSN:2042-6496
Container-title:Food & Function
language:en
Short-container-title:Food Funct.

Author:

Yuan Fangzhou¹²³⁴⁵,Ahmed Ishfaq⁶⁷⁸⁹,Lv Liangtao⁶⁷⁸⁹,Li Zhaojie¹⁰¹¹⁹,Li Zhenxing⁶⁷⁸⁹^ORCID,Lin Hong⁶⁷⁸⁹,Lin Hang¹²⁸⁹,Zhao Jinxia¹²⁸⁹,Tian Shenglan⁶⁷⁸⁹,Ma Jiaju⁶⁷⁸⁹

Affiliation:

1. State Key laboratory of Dairy Biotechnology

2. Shanghai Engineering Research Center of Dairy Biotechnology

3. Dairy Research Institute

4. Bright Dairy & Food Co. Ltd.

5. Shanghai 200436

6. College of Food Science and Engineering

7. Ocean University of China

8. Qingdao

9. P.R. China

10. Weihai Entry Exit Inspection and Quarantine Bureau

11. Weihai

12. The Affiliated Hospital of Medical College Qingdao University

Abstract

β-Lactoglobulin (β-LG) is recognized as the major milk allergen.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Medicine,Food Science

Link

http://pubs.rsc.org/en/content/articlepdf/2018/FO/C8FO00909K

Reference62 articles.

1. Bovine Milk Allergens: A Comprehensive Review

2. Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties

3. Epitopic characterization of native bovine β-lactoglobulin

4. Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound

5. Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin

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