02084nas a2200217   4500008004100000022001400041245012000055210006900175260007900244300001400323490000800337520126000345653001101605653002501616653001701641653001301658653002401671100002501695700002101720856012501741       2012                        eng d  a0273-228900aCharacterization of smallest active monomeric lipase from novel rhizopus strain: application in transesterification0 aCharacterization of smallest active monomeric lipase from novel   a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcAPR  a1769-17800 v1663 a<p>An extracellular lipase-producing fungus was isolated from oil-rich soil. This fungus belongs to the genus Rhizopus and clades with Rhizopus oryzae. Lipase was purified to homogeneity from this novel fungal source using ammonium sulphate precipitation followed by Q-Sepharose chromatography. The extracellular lipase was purified 8.6-fold, and enzymatic properties were studied. The molecular mass of the purified enzyme was estimated to be 17 kD by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and 16.25 kD by matrix-assisted laser desorption ionization/time-of-flight analysis. The native molecular mass was estimated to be 17.5 kD by gel filtration, indicating the protein to be monomer. The optimum pH and temperature for the enzyme catalysis were 7.0 A degrees C and 40 A degrees C, respectively. Enzyme was stable in pH range 6.0-7.0 and retains 95-100% activity when incubated at 50 A degrees C for 1 h. The pI of the purified lipase was 4.2. Enzyme was stable in the organic solvents such as ethanol, hexane and methanol for 2 h. Purified enzyme was used for transesterification of oleic acid in the presence of ethanol for production of oleic acid ethyl ester with a conversion efficiency of 66% after 24 h at 30 A degrees C.</p>10aLipase10aLow molecular weight10aPurification10aRhizopus10atransesterification1 aKantak, Jayshree, B.1 aPrabhune, Asmita  uhttps://library.ncl.res.in/content/characterization-smallest-active-monomeric-lipase-novel-rhizopus-strain-application-001448nas a2200193   4500008004100000022001400041245010500055210006900160260007300229300001200302490000700314520068200321653003201003653002501035653003401060100001801094700001401112856012801126       2012                        eng d  a0141-813000aSlow-tight binding inhibition of pepsin by an aspartic protease inhibitor from streptomyces sp MBR040 aSlowtight binding inhibition of pepsin by an aspartic protease i  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcJUL  a165-1740 v513 a<p>The present article reports a low molecular weight aspartic protease inhibitor from a Streptomyces sp. MBR04 exhibiting a two-step inhibition mechanism against pepsin. The kinetic interactions revealed a reversible, competitive, slow-tight binding inhibition with an IC50 and K-i values of 4.5 nM and 4 nM respectively. The conformational changes induced upon inhibitor binding to pepsin was monitored by far and near UV analysis, demonstrated that the inhibitor binds to the active site and causes inactivation. Chemical modification of the inhibitor with WRK and TNBS abolished the antiproteolytic activity of the inhibitor. (c) 2012 Elsevier B.V. All rights reserved.</p>10aAspartic protease inhibitor10aLow molecular weight10aSlow-tight binding inhibition1 aMenon, Vishnu1 aRao, Mala  uhttps://library.ncl.res.in/content/slow-tight-binding-inhibition-pepsin-aspartic-protease-inhibitor-streptomyces-sp-mbr04-0