01625nas a2200205   4500008004100000022001400041245008800055210006900143260009900212300001400311490000800325520083300333653001801166653002201184653002701206100001901233700003001252700002001282856011701302       2009                        eng d  a0960-852400aPurification and characterization of acidic lipase from aspergillus niger NCIM 12070 aPurification and characterization of acidic lipase from aspergil  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcFEB  a1486-14900 v1003 a<p>An extracellular lipase from Aspergillus niger NCIM 1207 has been purified to homogeneity using ammonium sulfate precipitation followed by phenyl sepharose and Sephacryl-100 gel chromatography. This protocol resulted in 149 fold purification with 54% final recovery. The purified enzyme showed a prominent single band on SDS-PAGE. The purified enzyme is a monomeric protein of 32.2 kDa molecular weight and exhibits optimal activity at 50 degrees C. One interesting feature of this enzyme is its highly acidic pH optimum. The isoelectric point (pl) of lipase was 8.5. The purified lipase appears to be unique since it cleaved triolein at only 3-position releasing 1,2-diolein. Chemical modification studies revealed that His, Ser, Carboxylate and Trp are involved in catalysis. (c) 2008 Elsevier Ltd. All rights reserved.</p>10aAcidic lipase10aAspergillus niger10aPositional specificity1 aMhetras, Nutan1 aBastawade, Kulbhushan, B.1 aGokhale, D., V.  uhttps://library.ncl.res.in/content/purification-and-characterization-acidic-lipase-aspergillus-niger-ncim-1207-0