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Background Pardosa is the genus of wolf spiders erected by C. L. Koch, 1847, currently represented by 549 species worldwide and 40 species from India. Results The present investigation deals with the first report of Pardosa brevivulva (Tanaka, Bulletin of the Biogeographical Society of Japan 31:21-24, 1975) in India from the mango and soybean fields of Latur District, Maharashtra. The species level identification was carried out on the basis of morphological characters and 18S rRNA gene sequencing. The silk of Pardosa brevivulva (Tanaka, Bulletin of the Biogeographical Society of Japan 31:21-24, 1975) was tested for its antimicrobial potential against test microbes. The bioactive fraction of Pardosa brevivulva silk was characterized for antimicrobial compounds by FT-IR, 13C & 1H NMR, and C18 column RP-HPLC analysis. The silk was able to inhibit the growth of B. megaterium, S. typhi, K. pneumoniae, A. flavus, C. albicans, U. maydis, and A. solani. Conclusion It can be surmised from the present investigation that the Pardosa brevivulva silk has good antimicrobial potential with useful bactericidal and fungicidal properties.

Hyperthermostable alkaline lipase fromBacillus sonorensis4R was purified and characterized. The enzyme production was carried out at 80°C and 9.0 pH in glucose-tween inorganic salt broth under static conditions for 96 h. Lipase was purified by anion exchange chromatography by 12.15 fold with a yield of 1.98%. The molecular weight of lipase was found to be 21.87 KDa by SDS-PAGE. The enzyme activity was optimal at 80°C witht1/2of 150 min and at 90°C, 100°C, 110°C, and 120°C; the respective values were 121.59 min, 90.01 min, 70.01 min, and 50 min. The enzyme was highly activated by Mg andt1/2values at 80°C were increased from 150 min to 180 min when magnesium and mannitol were added in combination. The activation energy calculated from Arrhenius plot was 31.102 KJ/mol. At 80–120°C, values ofΔHandΔGwere in the range of 28.16–27.83 KJ/mol and 102.79 KJ/mol to 111.66 KJ/mol, respectively. Lipase activity was highest at 9.0 pH and stable for 2 hours at this pH at 80°C. Pretreatment of lipase with MgSO4and CaSO4stimulated enzyme activity by 249.94% and 30.2%, respectively. The enzyme activity was greatly reduced by CoCl2, CdCl2, HgCl2, CuCl2, Pb(NO3)2, PMSF, orlistat, oleic acid, iodine, EDTA, and urea.