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Oat starch plays a crucial role in the stability of oat milk. Enzyme-hydrolyzed oat starch has been demonstrated to be an effective means of improving the stability of oat milk. The effects of different enzyme combinations on the stability of oat milk and the properties of starch in oats were investigated by adding α-amylase, amyloglucosidase, and different ratios of pullulanase and isoamylase. The results showed that as the degree of hydrolysis increased, the molecular weight, amylose content, and side chain length distribution of the starch decreased significantly. Moreover, compared with oat starch, the rheological and emulsifying properties of the starch hydrolysates were improved, and the characterization of emulsion stability showed that a 1:2 ratio of pullulanase to isoamylase promoted effective debranching and thus improved the stability of oat milk. This study demonstrated that debranching enzymes enhance the enzymatic hydrolysis of beverages and improve the physicochemical properties and stability of oat milk.
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http://dx.doi.org/10.3390/foods14071271 | DOI Listing |
Food Res Int
November 2025
School of Life and Health Sciences, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei Key Laboratory of Industrial Microbiology, Cooperative Innovation Center of Industrial Fermentation (Ministry of Education & Hubei Province), Hubei University of Technology, Wuhan, Hubei 430
This study aimed to examine the impact of composite enzymatic treatment on the physicochemical properties of oat milk, which would provide an effective strategy to improve the stability of plant-based milk. Oat milks treated with individual α-amylase or in combination with the protein glutaminase were produced. The result indicated that composite enzyme treatment significantly changed the physicochemical properties and significantly improved the stability of oat milk.
View Article and Find Full Text PDFFood Chem X
August 2025
Tianjin Institute of Industrial Biotechnology, Chinese Academy of Science, Tianjin 300308, China.
In this study, tannic acid (TA) was applied to remodel the structure of quercetin-loaded oat globulin fibrils (UF-Que), to form novel fibril-based composite hydrogels (UF-Que-TA) to encapsulate Que. The hydrogels were prepared by varying the [TA]/[UF] ratio to investigate the impact of TA on gelation behavior, microstructure, molecular interactions, and stability of Que. Physicochemical results indicated that the incorporation of TA significantly enhanced the gel strength and promoted non-covalent interactions including hydrogen bonding, hydrophobic interactions, and ionic interactions.
View Article and Find Full Text PDFPlants (Basel)
August 2025
Key Laboratory of Superior Forage Germplasm in the Qinghai-Tibetan Plateau, Qinghai Academy of Animal Science and Veterinary Medicine, Qinghai University, Xining 810016, China.
Oat is a dual-purpose crop valued for both grain and forage. The stay-green (SG) trait, which delays leaf senescence and prolongs photosynthesis, has been shown to increase yield and quality in several crop species, yet its performance across diverse environments in oats remains underexplored. In this study, multi-location field trials were conducted in Ledu, Huangzhong and Haiyan, Qinghai Province, China, to comprehensively evaluate the performance of stay-green oat lines.
View Article and Find Full Text PDFInorg Chem
August 2025
Department of Chemistry, Brown University, Providence, Rhode Island 02912, United States.
Nitrate (NO) and perchlorate (ClO) are persistent groundwater contaminants due to their high stability and solubility. Microorganisms reduce these anions using molybdenum-containing enzymes such as nitrate reductases and perchlorate reductases. Reported here is a bioinspired dinuclear Mo(V) catalyst, [MoO(L)(THF)] (), where L = 5-Bromo-2-hydroxybenzaldehyde thiosemicarbazone, and its reactivity with nitrate and perchlorate.
View Article and Find Full Text PDFDalton Trans
August 2025
Institute of Chemistry, Inorganic Chemistry, University of Graz, 8010 Graz, Austria.
Tungsten model complexes that replicate aspects of enzymatic activity are scarce due to challenges in reducing the readily prepared WO moiety. As a result, studies of bioinspired catalytic cycles remain limited, since tungsten in nature primarily facilitates redox processes such as Oxygen Atom Transfer (OAT). In our group, we recently observed that pyridine-2-thiolate (PyS)-supported tungsten dioxido complexes can be reduced to phosphine-stabilized W(IV) compounds, opening up opportunities for investigating rarely observed reduced participants in the OAT catalytic cycles.
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