Search Results (4)

The demand for bioactive molecules with nutritional benefits and pharmaceutically important properties is increasing, leading researchers to develop modified production strategies with low-cost purification processes. Recent developments in bioreactor technology can aid in the production of valuable products. Enzyme membrane bioreactors (EMRs) are emerging as sustainable synthesis processes in various agro-food industries, biofuel applications, and waste management processes. EMRs are modified reactors used for chemical reactions and product separation, particularly large-molecule hydrolysis and the conversion of macromolecules. EMRs generally produce low-molecular-weight carbohydrates, such as oligosaccharides, fructooligosaccharides, and gentiooligosaccharides. In this review, we provide a comprehensive overview of the use of EMRs for the production of valuable products, such as oligosaccharides and oligodextrans, and we discuss their application in the bioconversion of inulin, lignin, and sugars. Furthermore, we critically summarize the application and limitations of EMRs. This review provides important insights that can aid in the production of valuable products by food and pharmaceutical industries, and it is intended to assist scientists in developing improved quality and environmentally friendly prebiotics using EMRs. Full article

Gentiooligosaccharides (GnOS) are a kind of oligosaccharide formed by glucose with β-1-6 glycosidic bonds, which has become a new type of functional oligosaccharide for its unique refreshing bitter taste and valuable probiotic effects. However, the research on the enzymatic preparation of GnOS is not thorough enough. In this study, a GH1 thermophilic β-glucosidase from Thermotoga sp. KOL6 was used as a biocatalyst for the synthesis of GnOS. TsBgl1 exhibited excellent thermophilic and thermostable properties by possessing a melting temperature of 101.5 °C and reacting at 80–90 °C efficiently. Its half-life at 90 °C was approximately 5 h, suggesting its high heat resistance as well. TsBgl1 also showed excellent glucose tolerance with an inhibition constant (K_i) of 1720 mM and was stimulated in the presence of 0–900 mM glucose. TsBgl1 showed the highest hydrolytic activity on laminaribiose (Glc-β-1,3-Glc), but mainly synthetized gentiobiose (Glc-β-1,6-Glc) during transglycosylation. By optimizing the reaction conditions and substrate concentration, the highest yield of GnOS synthesized by TsBgl1 reached 144.3 g·L⁻¹ when 1000 g·L⁻¹ glucose was used as a substrate, which was higher than the highest yield ever reported. The thermophilic and thermostable properties of TsBgl1 were considered to be significant advantages in the industrial production of GnOS, where long periods of high-temperature reactions are required. This study was expected to provide an excellent candidate enzyme for industrial production of GnOS and also provide a reference for studying the transglycosylation of GH1 β-glucosidases. Full article

β-glucosidases can produce gentiooligosaccharides that are lucrative and promising for the prebiotic and alternative food industries. However, the commercial production of gentiooligosaccharides using β-glucosidase is challenging, as this process is limited by the need for high thermal energy and increasing demand for the enzyme. Here, a putative β-glucosidase gene, selected from the coral microbial metagenome, was expressed in Escherichia coli. Reverse hydrolysis of glucose by Blg163 at pH 7.0 and 40 °C achieved a gentiooligosaccharide yield of 43.02 ± 3.20 g·L⁻¹ at a conversion rate of 5.38 ± 0.40%. Transglycosylation of mixed substrates, glucose and cellobiose, by Blg163 consumed 21.6 U/0.5 g glucose/g cellobiose, achieving a gentiooligosaccharide yield of 70.34 ± 2.20 g·L⁻¹ at a conversion rate of 15.63%, which is close to the highest yield reported in previous findings. Blg163-mediated synthesis of gentiooligosaccharides is the mildest reaction and the lowest β-glucosidase consumption reported to date. Full article

The synthesis of gentiooligosaccharides of genistein and glycitein using cultured cells of Eucalyptus perriniana as biocatalysts was investigated. The cells of E. perriniana glycosylated genistein and glycitein to give the corresponding 4'-O-b-glucosides, 7-O-b-glucosides, and 7-O-b-gentiobiosides, which were two new compounds. The b-glucosides of genistein and glycitein showed 2,2-diphenyl-1-picrylhydrazyl (DPPH) free-radical scavenging activity and superoxide-radical scavenging activity. On the other hand, 7-O-b-glucosides of genistein and glycitein and the 7-O-b-gentiobioside of glycitein exerted inhibitory effects on IgE antibody production. Full article