Evidence map›Paper›PMID 40027172›Full record

ArticleLebensmittel-Wissenschaft + [i.e. und] Technologie. Food science + technology. Science + technologie alimentaire2025

Enzyme immobilization with plant-based polysaccharides through complex coacervation.

Waritsara Khongkomolsakul, Eunhye Yang, Younas Dadmohammadi, Hongmin Dong, Tiantian Lin, Yunan Huang, Alireza Abbaspourrad

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Article in Lebensmittel-Wissenschaft + [i.e. und] Technologie. Food science + technology. Science + technologie alimentaire, 2025. 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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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

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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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

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No citing paper in PubMed yet.

4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Waritsara KhongkomolsakulDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.
Eunhye YangDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.
Younas DadmohammadiDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.
Hongmin DongDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.
Tiantian LinDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.
Yunan HuangDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.
Alireza AbbaspourradDepartment of Food Science, College of Agriculture and Life Sciences, Cornell University, 243 Stocking Hall, Ithaca, NY, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant-based polysaccharides (PSs) were used to immobilize phytase in a coacervate system. Molecular docking predicted the intermolecular interactions and conformations between the phytase and the polysaccharide and correlated them to the activity recovery of phytase in the coacervate complex. PSs with two different functional groups, sulfate (iota (IC), lambda (LC), and kappa (KC) carrageenan) and carboxylate (low methoxyl pectin (LMP) and sodium alginate (SA)) were investigated. The optimized conditions for coacervation and activity recovery were pH 4 with a phytase-to-polysaccharide volume ratio of 12:1. Zeta potential measurements, FTIR spectroscopy, and molecular docking confirmed that electrostatic interactions and hydrogen bonding were the main driving forces for coacervate formation. Coacervate complexes of phytase formed with LMP, SA, or KC showed a high activity retention after immobilization, with approximately 30% yield of complex and 75% immobilization efficiency of the phytase. The lower enzyme activity retention observed for IC and LC complexes is attributed to these PSs binding to the enzyme's active site. Overall, this work contributes to the body of knowledge about intermolecular interactions between phytase and polysaccharides and can serve as a guide to formulating stable, functional ingredients for a plant-based diet.

Indexed as

Enzyme immobilizationMolecular dockingPhytasePolysaccharideProtein-polysaccharide intermolecular interaction

Identifiers

PMID40027172
PMCPMC11867993

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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.