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Boosting the catalytic efficiency of UGT51 for efficient production of rare ginsenoside Rh2.

Folia Microbiol (Praha)

January 2025

Biofuels Institute, School of Emergency Management, School of the Environment and Safety Engineering, Jiangsu University, Zhenjiang, 212013, China.

Ginsenoside Rh2(S) is well-known for its therapeutic potential against diverse conditions, including some cancers, inflammation, and diabetes. The enzymatic activity of uridine diphosphate glycosyltransferase 51 (UGT51) from Saccharomyces cerevisiae plays a pivotal role in the glycosylation process between UDP-glucose (donor) and protopanaxadiol (acceptor), to form ginsenoside Rh2. However, the catalytic efficiency of the UGT51 has remained a challenging task.

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When the kidneys are injured, uremic toxins (UTXs) accumulate in the body, affecting other tissues and causing a loss of essential body functions. This study investigated the adsorption of blood plasma-laden UTXs on the surface of PCL fibers to assess their potential as an alternative to membrane dialysis materials. Using plasma containing 26 UTXs at a concentration similar to that found in end-stage kidney disease patients, we analyzed the adsorbed proteins and examined clot formation in normal and toxin-treated plasma in the presence of PCL fibers.

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Combining Hard Shell with Soft Core to Enhance Enzyme Activity and Resist External Disturbances.

Adv Sci (Weinh)

January 2025

Department of Cardiology, The First People's Hospital of Wenling, Wenling Hospital of Wenzhou Medical University, Wenling, Zhejiang, 317500, China.

Immobilizing enzymes onto solid supports having enhanced catalytic activity and resistance to harsh external conditions is considered as a promising and critical method of broadening enzymatic applications in biosensing, biocatalysis, and biomedical devices; however, it is considerably hampered by limited strategies. Here, a core-shell strategy involving a soft-core hexahistidine metal assembly (HmA) is innovatively developed and characterized with encapsulated enzymes (catalase (CAT), horseradish peroxidase, glucose oxidase (GOx), and cascade enzymes (CAT+GOx)) and hard porous shells (zeolitic imidazolate framework (ZIF), ZIF-8, ZIF-67, ZIF-90, calcium carbonate, and hydroxyapatite). The enzyme-friendly environment provided by the embedded HmA proves beneficial for enhanced catalytic activity, which is particularly effective in preserving fragile enzymes that will have been deactivated without the HmA core during the mineralization of porous shells.

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Pickering Emulsions as Catalytic Systems in Food Applications.

ACS Food Sci Technol

January 2025

Department of Food Technology, Engineering and Science, Universitat de Lleida - Agrotecnio CeRCA Center, Avda. Alcalde Rovira Roure 191, 25198 Lleida, Spain.

Enzyme catalysis is important in food processing, such as in baking, dairy, and fiber processing and beverages. A recent advancement in catalysis is the development of Pickering emulsions as enzymatic catalytic systems; however, the use of Pickering emulsions (PEs) as catalytic systems in foods remains largely underdeveloped. Challenges exist that inhibit the widespread adoption of PEs as catalytic systems in foods.

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Biomimetic bioreactor for potentiated uricase replacement therapy in hyperuricemia and gout.

Front Bioeng Biotechnol

January 2025

Department of Rheumatology and Immunology, The Third Affiliated Hospital of Southern Medical University, Institute of Clinical Immunology, Academy of Orthopedics, Guangzhou, Guangdong, China.

Introduction: Uricase replacement therapy is a promising approach for managing hyperuricemia and gout but is hindered by challenges such as short blood circulation time, reduced catalytic activity, and excessive hydrogen peroxide (HO) production. These limitations necessitate innovative strategies to enhance therapeutic efficacy and safety.

Methods: We designed and synthesized RBC@SeMSN@Uri, a red blood cell-coated biomimetic self-cascade bioreactor, which encapsulates uricase (Uri) and a selenium-based nano-scavenger (SeMSN) within RBC membranes.

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