Many aquatic snails act as intermediate hosts for the larvae of trematodes, Fasciola hepatica and Fasciola gigantica, which cause the diseases fascioliasis and schistosomiasis. The WHO has tested several thousands of synthetic compounds for the control of the snail host. Although effective, these molluscicides have so far not proved themselves to be entirely satisfactory. With a growing awareness of environmental pollution, efforts are being made to discover molluscicidal products of plant origin. Being products of biosynthesis, these are potentially biodegradable in nature. Several groups of compounds present in various plants have been found to be toxic to target organisms at acceptable doses ranging from <1 to 100 ppm. Common medicinal plants, i.e. Thevetia peruviana, Alstonia scholaris (Family; Apocynaceae), Euphorbia pulcherima and Euphorbia hirta (Family; Euphorbiaceae), have potent molluscicidal activity against freshwater snails. The toxicological actions of Thevetia peruviana may be due to the presence of apigenin-5-methyl ether (flavonoid) and triterpenoid glycosides, while a number of alkaloids (pseudo-akuammigine in addition to betulin, ursolic acid and beta-sitosterol), steroids and triterpenoids are present in Alstonia scholaris and the diterpenoids, pulcherrol, beta-sitosterol, hentriacontane, ellagic acid and beta-amyrin are present in Euphorbia hirta and in Euphorbia pulcherima. Although, at present very little literature is available on the control of vector snails through plant origin pesticides, an attempt has been made in this review to assemble all the known information on molluscicidal properties of common medicinal plants of eastern Uttar Pradesh, India, which might be useful for the control of harmful snails.

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The culture conditions for maximum secretion of laccase by Loweporus lividus MTCC-1178 have been optimized. The laccase from the culture filtrate of L. lividus MTCC-1178 has been purified to homogeneity. The molecular weight of the purified laccase is 64.8 kDa. The enzymatic characteristics like K(m), pH, and temperature optimum using 2,6-dimethoxyphenol have been determined and found to be 480 microM, 5.0, and 60 degrees C, respectively. The K(m) values for other substrates like catechol, m-cresol, pyrogallol, and syringaldazine have also been determined and found to be 230, 210, 320, and 350 microM, respectively.

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A laccase has been purified from the liquid culture growth medium containing bagasse particles of Fomes durissimus. The method involved concentration of the culture filtrate by ultrafiltration and anion exchange chromatography on diethyl aminoethyl cellulose. The sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and native polyacrylamide gel electrophoresis both gave single protein band indicating that the enzyme preparation was pure. The molecular mass of the purified laccase determined from SDS-PAGE analysis was 75 kDa. Using 2,6-dimethoxyphenol as the substrate, the determined K (m) and k (cat) values of the laccase are 182 μM and 0.35 s(-1), respectively, giving a k (cat)/K (m) value of 1.92 × 10(3) M(-1) s(-1). The pH and temperature optimum were 4.0 and 35 °C, respectively. The purified laccase has yellow colour and does not show absorption band around 610 nm found in blue laccases. Moreover, it transformed methylbenzene to benzaldehyde in the absence of mediator molecules, property exhibited by yellow laccases.