Silver nanoparticles (AgNPs) were rapidly synthesized using an exopolysaccharide from Arthrobacter sp. B4 (B4-EPS). The optimum condition for AgNPs synthesis was under the concentration of 5 g/L B4-EPS and 1 mM AgNO₃ at 80°C between pH 7.0 and 8.0. The resulting AgNPs displayed a face-centred-cubic structure with the size range from 9 nm to 72 nm. Further analysis showed that flocculation and reduction of B4-EPS played a pivotal role in the formation of AgNPs. Furthermore, these nanoparticles exhibited great stability, excellent antimicrobial activity, and low phytotoxicity. The aforementioned data provide a feasible and efficient approach for green synthesis of AgNPs using microbial polysaccharides with flocculation and reduction activity, which will be promising in medical filed.

The novel exopolysaccharide HZ-7 is produced by Klebsiella sp. H-207, and its fermentation conditions were optimized by response surface methodology (RSM). In this study, the optimized medium consisted of sucrose 31.93 g/L, KNO₃ 2.17 g/L and K₂HPO₄ 5.47 g/L; while the optimized culture conditions consisted of seed age 13 h, with an inoculum size of 10.6% and incubation temperature of 28.9°C. A maximum HZ-7 yield of about 15.05 g/L was achieved under the optimized conditions using RSM and single-factor experiments. Next the exopolysaccharide HZ-7 was partially purified and characterized. The resulting product showed good properties, such as high concentration of uronic acid (41.67%), low average molecular weight (about 1.94×10⁵ Da) and porous surface structure, were very advantageous to biosorption. Therefore HZ-7 was applied to absorb hexavalent chromium (Cr(VI)). The maximum adsorption efficiency (99.2%) which was obtained at an initial pH of 1.0 along with an initial Cr(VI) concentration of 20 mg/L, was not affected by ordinary metal ions and temperature. These data suggest Klebsiella sp. H-207 exopolysaccharide will be promising potential for industrial application.

Pectate lyase (EC 4.2.2.2) catalyzes the cleavage of α-1,4-glycosidic bonds of pectin polymers, and it has potential uses in the textile industry. In this study, a novel pectate lyase belonging to polysaccharide lyase family 10 was screened from the secreted enzyme extract of Paenibacillus polymyxa KF-1 and identified by liquid chromatography-MS/MS. The gene was cloned from P. polymyxa KF-1 genomic DNA and expressed in Escherichia coli. The recombinant enzyme PpPel10a had a predicted Mr of 45.2 kDa and pI of 9.41. Using polygalacturonic acid (PGA) as substrate, the optimal conditions for PpPel10a reaction were determined to be 50 °C and pH 9.0, respectively. The K_m, v_max and k_cat values of PpPel10a with PGA as substrate were 0.12 g/L, 289 μmol/min/mg, and 202.3 s⁻¹, respectively. Recombinant PpPel10a degraded citrus pectin, producing unsaturated mono- and oligogalacturonic acids. PpPel10a reduced the viscosity of PGA, and weight loss of ramie (Boehmeria nivea) fibers was observed after treatment with the enzyme alone (22.5%) or the enzyme in combination with alkali (26.3%). This enzyme has potential for use in plant fiber processing.