@article { ISI:000261569100072,
	title = {Purification and characterization of acidic lipase from aspergillus niger NCIM 1207},
	journal = {Bioresource Technology},
	volume = {100},
	number = {3},
	year = {2009},
	month = {FEB},
	pages = {1486-1490},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<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>},
	keywords = {Acidic lipase, Aspergillus niger, Positional specificity},
	issn = {0960-8524},
	doi = {10.1016/j.biortech.2008.08.016},
	author = {Mhetras, Nutan and Bastawade, Kulbhushan B. and Gokhale, D. V.}
}
@article {43594,
	title = {Purification and characterization of an extracellular beta-xylosidase from Pseudozyma hubeiensis NCIM 3574 (PhXyl), an unexplored yeast},
	journal = {AMB Express},
	volume = {6},
	year = {2016},
	month = {SEP},
	pages = {Article Number: 73},
	abstract = {This paper reports on the production of beta-xylosidase from an unexplored yeast, Pseudozyma hubeinsis. The expression of this enzyme could be induced by beech wood xylan when the yeast was grown at 27 degrees C. The enzyme was purified to homogeneity as a glycoprotein with 23 \% glycosylation. The purification protocol involved ammonium sulphate precipitation, QAE-Sephadex A50 ion exchange chromatography and sephacryl-200 column chromatography which resulted in 8.3-fold purification with 53.12 \% final recovery. The purified enzyme showed prominent single band on SDS-PAGE. It is a monomeric protein of 110 kDa molecular weight confirmed by SDS-PAGE followed by MALDI-TOF mass spectrometry (112.3 kDa). The enzyme was optimally active at 60 degrees C and pH 4.5 and stable at pH range (4-9) and at 50 degrees C for 4 h. Chemical modification studies revealed that active site of the purified enzyme comprised of carboxyl, tyrosine and tryptophan residues. The carboxyl residue is involved in catalysis and tryptophan residue is solely involved in substrate binding. The best match from the search of the NCBInr database was with gi vertical bar 808364558 glycoside hydrolase of Pseudozyma hubeiensis SY62 with 26 \% sequence coverage confirming that it is a glycoside hydrolase/beta-glucosidase. From the search of customized SWISSPROT database, it was revealed that SWISSPROT does not contain any entries that are similar to the purified enzyme.},
	doi = {10.1186/s13568-016-0243-7},
	author = {Mhetras, Nutan and Liddell, Susan and Gokhale, Digambar}
}
