Endovascular treatment of deep, stomach aneurysms and also pseudoaneurysms.

The effect of heat moisture treatment (HMT) and annealing (ANN) on physicochemical and rheological properties and in vitro digestibility of starch extracted from sohphlang (Flemingia vestita) was studied. Modification by HMT and ANN increased amylose content and water absorption capacity. For all modified samples, solubility, swelling power and amylose leaching progressively increased with increasing temperature (50-90 °C). Modified starches exhibited higher contents of SDS and RS and lower content of RDS as compared to native starch for both cooked and uncooked samples. The rheological properties of starch pastes were investigated by the power law model. The starch paste samples exhibited shear thinning characteristics and phase angle was closer to 0°. HMT-30 and ANN-80 exhibited greater impact on in vitro digestibility and rheological behaviour among the HMT and ANN starches, respectively. Thus, ANN and HMT could be used for modification of sohphlang starch making them suitable for application in food systems like pasta and noodles.The Nocardiopsis alba strain OM-5 showed maximum protease production in submerged culture. The OM-5 protease was purified by hydrophobic interaction chromatography. The purified protease of 68 kDa showed maximum activity (3312 ± 1.64 U/mL) at 70 °C and was quite stable at 80 °C up to 4 M NaCl (w/v) at pH 9. The purified protease showed significant activity and stability in different cations, denaturing agents, metal ions, and osmolytes. The thermodynamic parameters including deactivation rate constant (Kd) and half lives (t1/2) at 50-80 °C were in the range of 2.50 × 10-3 to 5.50 × 10-3 and 277.25-111.25 min respectively at 0-4 M NaCl. The structural stability of the OM-5 protease under various harsh conditions was elucidated by circular dichroism (CD) spectroscopy followed by K2D3 analysis revealed that the native structure of OM-5 protease was stable even in sodium dodecyl sulfate and Tween 20 indicated by increased α-helices content assisted with decreased β-sheets content.This study aimed to investigate the molecular characterization, antioxidant activity in vitro, cytotoxicity study of an exopolysaccharide isolated from Citrobacter freundii. Tipiracil mw Firstly, the culture conditions were standardized by the Design of experiments (DoE) based approach, and the final yield of thecrude exopolysaccharide was optimized at 2568 ± 169 mg L-1. One large fraction of exopolysaccharide was obtained from the culture filtrate by size exclusion chromatography and molecular characteristics were studied. A new mannose rich exopolysaccharide (Fraction-I) with average molecular weight ~ 1.34 × 105 Da was isolated. The sugar analysis showed the presence of mannose and glucose in a molar ratio of nearly 72 respectively. The structure of the repeating unit in the exopolysaccharide was determined through chemical and 1D/2D- NMR experiments as Finally, the antioxidant activity, and the cytotoxicity of the exopolysaccharide were investigated and the relationship with molecular properties was discussed as well.Bacterial cellulose (BC) has received immense interest in medical, pharmaceutical, and other related fields owing to its intrinsic physical, mechanical, and biological features. Its structural features offer an ideal environment for developing composites, thereby further extending its areas of applications. BC was initially used in wound dressing, artificial blood vessels, organ development, and tissue regeneration; however, the recent focus has switched to 3D printing techniques. BC can serve as suitable material for treating different cancers due to unique liquid absorbing and drug loading properties. BC-based scaffolds have been synthesized and tested for in vitro culturing of cancer cells to simulate tumor microenvironments. These scaffolds support normal growth of cancer cells, particularly breast and ovarian cancer cells, showing significant adhesion, proliferation, ingrowth, and differentiation. This review describes the different approaches of manipulating BC for use in medicine, with particular focus on the applications of BC composites in cancer treatment. A detailed discussion about various formulations of BC in multiple cancer therapeutics is summarized.Only a few known epoxide hydrolases (EHs) displayed activity towards o-nitrostyrene oxide (4a), presumably owing to the large steric hindrance caused by o-nitro substituent. Therefore, excavating EHs with high activity and enantio- and/or regio-selectivity towards racemic (rac-) 4a is essential but challenging. Here, AuEH2 from Aspergillus usamii was expressed in E. coli BL21(DE3). E. coli/Aueh2, an E. coli transformant expressing AuEH2, possessed EH activities of 16.2-184 U/g wet cell towards rac-styrene oxide (1a) and its derivatives (2a-13a), and the largest enantiomeric ratio of 96 towards rac-4a. The regioselectivity coefficients, βR and βS, of AuEH2 were determined to be 99.2% and 98.9%, suggesting that it regiopreferentially attacks the Cβ in the oxirane rings of (R)- and (S)-4a. Then, the nearly perfect kinetic resolution of 20 mM rac-4a in pure water was carried out using 20 mg/mL wet cells of E. coli/Aueh2 at 25 °C for 50 min, retaining (S)-4a with over 99% ees and 48.9% yields, while producing (R)-o-nitrophenyl-1,2-ethanediol (4b) with 95.3% eep and 49.8% yieldp. To elucidate the molecular mechanism of AuEH2 with high enantiopreference for (R)-4a, its crystal structure was solved by X-ray diffraction and the molecular docking of AuEH2 with (R)- or (S)-4a was simulated.Lignocellulosic biomass (LCB) is a prominent option for second-generation biofuels production. Cellulase hydrolyses cellulose, a component of LCB by attacking the β-1,4-glycosidic bonds, thus liberating mono, di, and oligosaccharides, which subsequently, can be converted to biofuel. In this study, a novel cellulase (Cel-3.1) of 1593 bp which encodes a 530 amino acid protein was identified from buffalo rumen metagenomic fosmid library, and functional expression was achieved through transformation into Escherichia coli. The molecular weight was estimated as 58 kDa on SDS-PAGE. Cel-3.1 belongs to glycosyl hydrolase family-5 (GH-5) and is predicted to have 14 α-helices and 15 β-strands. The optimal temperature and pH for Cel-3.1 were experimentally determined as 5.0 and 50 °C respectively. The synergistic effect of Ca2+ with K+ ions improved Cel-3.1 activity significantly (25%) and 1% Polyethylene Glycol (PEG-400), 1% β-mercaptoethanol enhanced the relative activity Cel-3.1 by 31.68%, 12.03% respectively. Further, the enzymatic (Cel-3.Tipiracil mw