Glycosylation Remodeling and Thermal Denaturation Dictate the Functional Diversification of Protein Z.

Jianyu Yang, Xiaoqi Zhang, Tuo Zhang, Huijuan Zhang, Zengwang Guo, Chenyan Lv

Abstract read

In one paragraph

Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Jianyu YangCollege of Food Science, Northeast Agricultural University, Harbin 150030, China.

Xiaoqi ZhangBeijing Key Laboratory of Functional Food from Plant Resources, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China.

Tuo ZhangBeijing Key Laboratory of Functional Food from Plant Resources, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China.

Huijuan ZhangSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, China.ORCID 0000-0003-3060-4246

Zengwang GuoCollege of Food Science, Northeast Agricultural University, Harbin 150030, China.

Chenyan LvBeijing Key Laboratory of Functional Food from Plant Resources, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China.ORCID 0000-0003-2957-3614

Funding

National Natural Science Foundation of China 32272304

6 · The paper itself

Abstract

Protein Z (PZ) derived from barley malt has been identified as one of the key proteins contributing to foam stability. Recently, PZ was also recognized as an effective carrier, a functionality attributed to its serpin-like activities. This study investigated key structural-functional changes in PZ during thermal processing (mashing and boiling). The structural modifications of PZ variants were analyzed using FT-IR (Fourier Transform Infrared Spectroscopy). The results indicated that the secondary structure of PZ, after mashing, did not change significantly, whereas the β-turn content of PZ after boiling increased to 24.08% ± 0.34%. Interfacial adsorption kinetics, coupled with structural analysis, revealed that PZ, after mashing, exhibited the highest foamability (41.4 ± 0.38%), which was associated with the highest diffusion rate constant (K

Indexed as

beer productionfoaming propertiesserpinstructure of proteinthrombin inhibitory ability

Identifiers

PMID41829126

DOI10.3390/foods15050853

PMCPMC12984823

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LicenceCC BY

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.