Jack Yang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Jack Yang has a total of 103 co-authors. Here are the top co-authors by number of shared publications:
- Leonard Martin C. Sagis
Laboratory of Physics and Physical Chemistry of Foods, Wageningen University, Bornse Weilanden 9, 6708, WG, Wageningen, the Netherlands
22 shared publications Constantinos V. Nikiforidis
9 shared publicationsErik van der Linden
7 shared publicationsLeonard M.C. Sagis
Laboratory of Physics and Physical Chemistry of Foods, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands
7 shared publicationsPaul Venema
5 shared publications- Constantinos V. Nikiforidis
Biobased Chemistry and Technology, Wageningen University and Research, Bornse Weilanden 9, PO Box 17, 6708 WG, Wageningen, the Netherlands
4 shared publications
Latest Publications
- Open Access
- 5 October 2026
- Published by Elsevier in Advances in Colloid and Interface Science
- Vol. 358
The Interface Science Data Repository: A (meta)data framework and platform for FAIR data reporting in experimental fluid interface science
- 5 October 2026
- Published by Elsevier in Advances in Colloid and Interface Science
- Vol. 358
Open AccessThe Interface Science Data Repository: A (meta)data framework and platform for FAIR data reporting in experimental fluid interface science
- Open Access
- 29 July 2026
- Published by Elsevier in Food Hydrocolloids
- Vol. 183
Solubility and aggregation state govern foam performance of lab-extracted and commercial soy proteins
- 29 July 2026
- Published by Elsevier in Food Hydrocolloids
- Vol. 183
Open AccessSolubility and aggregation state govern foam performance of lab-extracted and commercial soy proteins
- Open Access
- 16 July 2026
- Published by Elsevier in Food Hydrocolloids
- Vol. 183
Using glutaminase enzyme treatment to alter oil-water interfacial and emulsifying properties of heated pea proteins
- 16 July 2026
- Published by Elsevier in Food Hydrocolloids
- Vol. 183
Open AccessUsing glutaminase enzyme treatment to alter oil-water interfacial and emulsifying properties of heated pea proteins
- Open Access
- 19 May 2026
- Published by Elsevier in Food Hydrocolloids
- Vol. 180
The effect of sucrose on commercial faba bean protein foaming properties
- 19 May 2026
- Published by Elsevier in Food Hydrocolloids
- Vol. 180
Open AccessThe effect of sucrose on commercial faba bean protein foaming properties
- Open Access
- 6 December 2025
- Published by Elsevier in Current Research in Food Science
- Vol. 12
Lubrication by plant-based emulsions: Linking oil-water protein-stabilized interfacial mechanical properties to oil droplet lubrication properties
- 6 December 2025
- Published by Elsevier in Current Research in Food Science
- Vol. 12
Open AccessLubrication by plant-based emulsions: Linking oil-water protein-stabilized interfacial mechanical properties to oil droplet lubrication properties
- Open Access
- 8 August 2025
- Published by Elsevier in Food Chemistry
- Vol. 493 (Pt 2) , 145852
The digestibility of rapeseed protein isolate prepared by salt and alkali extraction: The importance of protein composition
- 8 August 2025
- Published by Elsevier in Food Chemistry
- Vol. 493 (Pt 2) , 145852
Open AccessThe digestibility of rapeseed protein isolate prepared by salt and alkali extraction: The importance of protein composition
- Open Access
- 13 December 2024
- Published by Elsevier in Journal of Colloid and Interface Science
- Vol. 683 (Pt 1) , 408-419
Thin liquid films stabilized by plant proteins: Implications for foam stability
- 13 December 2024
- Published by Elsevier in Journal of Colloid and Interface Science
- Vol. 683 (Pt 1) , 408-419
Open AccessThin liquid films stabilized by plant proteins: Implications for foam stability
- Open Access
- 17 October 2024
- Published by Elsevier in Food Hydrocolloids
- Vol. 160
Effect of membrane filtration and direct steam injection on mildly refined rapeseed protein solubility, air-water interfacial and foaming properties
- 17 October 2024
- Published by Elsevier in Food Hydrocolloids
- Vol. 160
Open AccessEffect of membrane filtration and direct steam injection on mildly refined rapeseed protein solubility, air-water interfacial and foaming properties
- Open Access
- 23 September 2024
- Published by Elsevier in Journal of Colloid and Interface Science
- Vol. 678 (Pt C) , 1077-1086
Modifying the interfacial dynamics of oleosome (lipid droplet) membrane using curcumin
- 23 September 2024
- Published by Elsevier in Journal of Colloid and Interface Science
- Vol. 678 (Pt C) , 1077-1086
Open AccessModifying the interfacial dynamics of oleosome (lipid droplet) membrane using curcumin
- Top Cited PapersOpen Access
- 8 September 2024
- Published by Wiley in Comprehensive Reviews in Food Science and Food Safety
- Vol. 23 (5) , e70015
Protein–phenolic interactions and reactions: Discrepancies, challenges, and opportunities
Although noncovalent interactions and covalent reactions between phenolic compounds and proteins have been investigated across diverse scientific disciplines, a comprehensive understanding and identification of their products remain elusive. This review will initially outline the chemical framework and, subsequently, delve into unresolved or debated chemical and functional food‐related implications, as well as forthcoming challenges in this topic. The primary objective is to elucidate the multiple aspects of protein–phenolic interactions and reactions, along with the underlying overwhelming dynamics and possibilities of follow‐up reactions and potential crosslinking between proteins and phenolic compounds. The resulting products are challenging to identify and characterize analytically, as interactions and reactions occur concurrently, mutually influencing each other. Moreover, they are being modulated by various conditions such as the reaction parameters and, obviously, the chemical structure. Additionally, this review delineates the resulting discrepancies and challenges of properties and attributes such as color, taste, foaming, emulsion and gel formation, as well as effects on protein digestibility and allergenicity. Ultimately, this review is an opinion paper of a group of experts, dealing with these challenges for quite a while and aiming at equipping researchers with a critical and systematic approach to address current research gaps concerning protein–phenolic interactions and reactions.
- 8 September 2024
- Published by Wiley in Comprehensive Reviews in Food Science and Food Safety
- Vol. 23 (5) , e70015
Top Cited PapersOpen AccessProtein–phenolic interactions and reactions: Discrepancies, challenges, and opportunities
Although noncovalent interactions and covalent reactions between phenolic compounds and proteins have been investigated across diverse scientific disciplines, a comprehensive understanding and identification of their products remain elusive. This review will initially outline the chemical framework and, subsequently, delve into unresolved or debated chemical and functional food‐related implications, as well as forthcoming challenges in this topic. The primary objective is to elucidate the multiple aspects of protein–phenolic interactions and reactions, along with the underlying overwhelming dynamics and possibilities of follow‐up reactions and potential crosslinking between proteins and phenolic compounds. The resulting products are challenging to identify and characterize analytically, as interactions and reactions occur concurrently, mutually influencing each other. Moreover, they are being modulated by various conditions such as the reaction parameters and, obviously, the chemical structure. Additionally, this review delineates the resulting discrepancies and challenges of properties and attributes such as color, taste, foaming, emulsion and gel formation, as well as effects on protein digestibility and allergenicity. Ultimately, this review is an opinion paper of a group of experts, dealing with these challenges for quite a while and aiming at equipping researchers with a critical and systematic approach to address current research gaps concerning protein–phenolic interactions and reactions.