ReviewComprehensive reviews in food science and food safety2026
Amylosucrase as a Versatile Biocatalyst for Next-Generation Functional Ingredients: Starch Modification and Glycoside Synthesis.
Review in Comprehensive reviews in food science and food safety, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Amylosucrase (ASase, E.C. 2.4.1.4) is a transglucosidase that catalyzes α-glucan synthesis and transglycosylation reactions using sucrose as the sole substrate. Unlike Leloir glycosyltransferases requiring expensive nucleotide sugars, ASases utilize readily available sucrose as a cost-effective glucose donor, offering economic advantages for industrial applications. This review comprehensively examines the current state of ASase research, covering structural characteristics, catalytic mechanisms, substrate specificities, and industrial applications. Major applications include the synthesis of functional carbohydrates, such as short-chain glucan microparticles for encapsulation and rare sugars (turanose and trehalulose), as well as starch modification for enhanced nutritional profiles. Furthermore, the enzyme plays a crucial role in generating α-glycosides of bioactive compounds, significantly improving their physicochemical stability and bioavailability. Recent advances in protein engineering have improved enzyme thermostability and expanded substrate scope, though challenges remain in industrial-scale implementation. Current limitations in enzyme stability and product yields are critically analyzed, alongside future research directions for improving catalytic performance and process economics. The diverse applications of ASases in food, nutraceutical, and cosmetic industries demonstrate their potential as versatile biocatalysts for producing functional ingredients with improved properties.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.