Individual modification site preferences of α-lactalbumin glycated in the dry state by glucose, maltotriose and galacturonic acid-Reference-Cited by-同舟云学术

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Individual modification site preferences of α-lactalbumin glycated in the dry state by glucose, maltotriose and galacturonic acid

Published:2024-06 Issue: Volume:4 Page:100657
ISSN:2772-753X
Container-title:Food Chemistry Advances
language:en
Short-container-title:Food Chemistry Advances

Author:

Cardoso H.B.,Deng Y.,Wierenga P.A.,Gruppen H.,Schols H.A.^ORCID

Funder

FrieslandCampina

Publisher

Elsevier BV

Reference23 articles.

1. Enzymic hydrolysis of food proteins;Adler-Nissen,1986

2. Modification of ovalbumin with oligogalacturonic acids through the Maillard reaction;Aoki;Food Research International,2001

3. Introducing enzyme selectivity: A quantitative parameter to describe enzymatic protein hydrolysis;Butre;Analytical and Bioanalytical Chemistry,2014

4. Influence of water availability on the enzymatic hydrolysis of proteins;Butre;Process Biochemistry,2014

5. Maillard induced saccharide degradation and its effects on protein glycation and aggregation;Cardoso;Food Chemistry Advances,2023

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