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1.
Carbohydr Polym ; 333: 121929, 2024 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-38494211

RESUMO

Polymerized guluronates (polyG)-specific alginate lyase with lower polymerized mannuronates (polyM)-degrading activity, superior stability, and clear action mode is a powerful biotechnology tool for the preparation of AOSs rich in M blocks. In this study, we expressed and characterized a polyG-specific alginate lyase OUC-FaAly7 from Formosa agariphila KMM3901. OUC-FaAly7 belonging to polysaccharide lyase (PL) family 7 had highest activity (2743.7 ± 20.3 U/µmol) at 45 °C and pH 6.0. Surprisingly, its specific activity against polyG reached 8560.2 ± 76.7 U/µmol, whereas its polyM-degrading activity was nearly 0 within 10 min reaction. Suggesting that OUC-FaAly7 was a strict polyG-specific alginate lyase. Importantly, OUC-FaAly7 showed a wide range of temperature adaptations and remarkable temperature and pH stability. Its relative activity between 20 °C and 45 °C reached >90 % of the maximum activity. The minimum identifiable substrate of OUC-FaAly7 was guluronate tetrasaccharide (G4). Action process and mode showed that it was a novel alginate lyase digesting guluronate hexaose (G6), guluronate heptaose (G7), and polymerized guluronates, with the preferential generation of unsaturated guluronate pentasaccharide (UG5), although which could be further degraded into unsaturated guluronate disaccharide (UG3) and trisaccharide (UG2). This study contributes to illustrating the catalytic properties, substrate recognition, and action mode of novel polyG-specific alginate lyases.


Assuntos
Dissacarídeos , Oligossacarídeos , Especificidade por Substrato , Oligossacarídeos/metabolismo , Dissacarídeos/metabolismo , Polissacarídeo-Liases/metabolismo , Alginatos/metabolismo , Concentração de Íons de Hidrogênio , Proteínas de Bactérias/química
2.
J Sci Food Agric ; 102(13): 5606-5617, 2022 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-35478460

RESUMO

α-Carotene, one of the C40 carotenes, is a natural lipid-soluble terpene. The chemical structure of α-carotene is based on the unsaturated polyene chain skeleton, with an ε-ring and a ß-ring on each side of the skeleton. α-Carotene is widely found in dietary fruits and vegetables, and the concentration depends on the plant species. In addition, processing methods and storage conditions used in the food and medical industries can alter the concentration of α-carotene in raw materials. This review of α-carotene summarizes the major studies on chemical structure, source, extraction, detection, biosynthesis, processing effect, bioactivity, medicine, and biotechnology. Whether α-carotene supplementation or a diet rich in fruits and vegetables has a positive effect on the prevention of cancer, cardiovascular disease, and other diseases is the focus of this study. © 2022 Society of Chemical Industry.


Assuntos
Pesquisa Biomédica , Luteína , Carotenoides/análise , Verduras/química
3.
Food Chem ; 349: 129209, 2021 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-33588184

RESUMO

Porphyra is one of the most economically important red algae in the world. The functional components extracted from Porphyra such as porphyrans, proteins, lipids, and minerals have strong physiological activities. Porphyran, a sulfated galactan, is composed of alternating 1,4-linked α-l-galactopyranose-6-sulfate (L6S) and 1,3-linked ß-d-galactopyranose (G). Porphyran and oligo-porphyran have a series of pharmacological and biological functions, such as antioxidation, anticancer, antiaging, antiallergic, immunomodulatory, hypoglycaemic, and hypolipidemic effects. Thus, red algae Porphyra-derived porphyran and oligo-porphyran have various potential applications in food, medicine, and cosmetic fields. For better application, this review introduces and summarizes the structure and source of porphyran as well as the preparation methods, biological activities, and potential applications of porphyran and oligo-porphyran. Moreover, the future research directions and emphasis of porphyran and oligo-porphyran preparation as well as their functional activities and applications are highlighted and prospected.


Assuntos
Polimerização , Porphyra/química , Sefarose/análogos & derivados , Antioxidantes/química , Antioxidantes/isolamento & purificação , Antioxidantes/farmacologia , Sefarose/química , Sefarose/isolamento & purificação , Sefarose/farmacologia
4.
Int J Biol Macromol ; 168: 663-675, 2021 Jan 31.
Artigo em Inglês | MEDLINE | ID: mdl-33220370

RESUMO

Given the excellent characteristics of alginate, it is an industrially important polysaccharide. Mannuronan C5-epimerase (MC5E) is an alginate-modifying enzyme that catalyzes the conversion of ß-D-mannuronate (M) to its C5 epimer α-L-guluronate (G) in alginate. Both the biological activities and physical properties of alginate are determined by M/G ratios and distribution patterns. Therefore, MC5E is regarded as a biotechnological tool for modifying and processing alginate. Various MC5Es derived from brown algae, Pseudomonas and Azotobacter have been isolated and characterized. With the rapid development of structural biology, the crystal structures and catalytic mechanisms of several MC5Es have been elucidated. It is necessary to comprehensively understand the research status of this alginate-modifying enzyme. In this review, the properties and potential applications of MC5Es isolated from different kinds of organisms are summarized and reviewed. Moreover, future research directions of MC5Es as well as strategies to enhance their properties are elucidated, highlighted, and prospected.


Assuntos
Alginatos/química , Carboidratos Epimerases/química , Carboidratos Epimerases/metabolismo , Azotobacter/enzimologia , Proteínas de Bactérias/metabolismo , Ácidos Hexurônicos/química , Conformação Proteica , Engenharia de Proteínas , Pseudomonas/enzimologia , Especificidade por Substrato
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