ArticleFoods (Basel, Switzerland)2021
Improved Performance of D-Psicose 3-Epimerase by Immobilisation on Amino-Epoxide Support with Intense Multipoint Attachment.
Article in Foods (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 18 citations in OpenAlex.
- Transforming monosaccharides: Recent advances in rare sugar production and future exploration.BBA advances · 2025Article
- Research Advances of d-allulose: An Overview of Physiological Functions, Enzymatic Biotransformation Technologies, and Production Processes.Foods (Basel, Switzerland) · 2021Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
D-allulose is an epimer of D-fructose at the C-3 position. With similar sweetness to sucrose and a low-calorie profile, D-allulose has been considered a promising functional sweetener. D-psicose 3-epimerase (DPEase; EC 5.1.3.30) catalyses the synthesis of D-allulose from D-fructose. Immobilised enzymes are becoming increasingly popular because of their better stability and reusability. However, immobilised DPEase generally exhibits less activity or poses difficulty in separation. This study aimed to obtain immobilised DPEase with high catalytic activity, stability, and ease of separation from the reaction solution. In this study, DPEase was immobilised on an amino-epoxide support, ReliZyme HFA403/M (HFA), in four steps (ion exchange, covalent binding, glutaraldehyde crosslinking, and blocking). Glycine-blocked (four-step immobilisation) and unblocked (three-step immobilisation) immobilised DPEase exhibited activities of 103.5 and 138.8 U/g support, respectively, but contained equal amounts of protein. After incubation at 60 °C for 2 h, the residual activity of free enzyme decreased to 12.5%, but the activities of unblocked and blocked DPEase remained at 40.9% and 52.3%, respectively. Immobilisation also altered the substrate specificity of the enzyme, catalysing L-sorbose to L-tagatose and D-tagatose to D-sorbose. Overall, the immobilised DPEase with intense multipoint attachment, especially glycine-blocked DPEase, showed better properties than the free form, providing a superior potential for D-allulose biosynthesis.
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