Search

The study aimed to investigate the impacts of a polysaccharide (BFP) from Bangia fusco-purpurea on high-fat diet (HFD)-induced obesity in C57BL/6 mice, as well as its underlying mechanisms. Our results showed that orally administrated BFP was more effective than inulin (INU) in reducing body weight and fat accumulation in obese mice, indicating its anti-obesity effect. BFP effectively improved the compositions and metabolites of intestinal microbiota in obese mice, leading to enhanced energy metabolism and lipid metabolism, thus contributing to its anti-obesity effect. Notably, the better anti-obesity effect of BFP compared to INU were attributed to their varying degrees of modulation of specific intestinal microbial taxa, such as Clostridium and Aerococcus, as well as the regulation of differential metabolites (including biotin, piperine, G6P, etc.) also varies. Also, both in vitro (3T3-L1 preadipocytes) and in vivo (HFD-induced obese mice) models confirmed that BFP achieved anti-obesity effect attributed to enhance energy metabolism, promote lipolysis, increase fatty acid oxidation, and inhibit adipogenesis via activating the AMP-activated protein kinase and Acetyl-CoA carboxylase signaling pathways and suppressing the peroxisome proliferator-activated receptor γ expression. Our findings suggest that BFP has the potential to be used as prebiotics, dietary agents, and nutritional supplements against obesity., Competing Interests: Declaration of competing interest The authors declare no conflict of interest., (Copyright © 2024. Published by Elsevier B.V.)

α-L-Rhamnosidase has attracted lots of attention due to its industrial potential applications. The applicability of α-L-rhamnosidase, however, was limited by their low ligand affinity on the industrial scale. In order to improve the affinity of α-L-rhamnosidase for industrial use, we investigated the variation of its affinity by amino acid replacement. Particularly, the enzyme affinity of a α-L-rhamnosidase from Aspergillus niger JMU-TS528 (rRha1) was measured with the semi-conservative amino acid (homology between 30% -80%) replaced. As a result, the enzyme affinity of the two mutants, R404S and N578D, were increased by 1.45-fold and 2.3-fold, respectively, showing that these two mutants could be the promising candidates for industrial use. To test if these mutations bring negative effect on the enzyme properties, we also determined the other enzymatic properties of these mutants and showed no negative effect. To understand the improvement of enzyme affinity, the conformational flexibility of (α/α) 6 -barrel catalytic domain were examined by molecular dynamics (MD) simulation, and demonstrated that the conformations of these mutants are more flexible, which could influence the affinity of substrates to the enzyme and hence the enzyme activity. This work not only enhanced the enzyme affinity of a α-L-rhamnosidase, making rRha1 a promising candidate for industrial processes, but also provided an effective technical strategy for improving affinity of other enzymes., Competing Interests: Declaration of competing interest The authors declare that they have no conflict of interest., (Copyright © 2020 Elsevier B.V. All rights reserved.)