A novel lipolytic activity of Rhodotorula glutinis cells: Production, partial characterization and application in the synthesis of esters

Hatzinikolaou, DG; Kourentzi, E; Stamatis, H; Christakopoulos, P; Kolisis, FN; Kekos, D; Macris, BJ

dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Kourentzi, E	en
dc.contributor.author	Stamatis, H	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kolisis, FN	en
dc.contributor.author	Kekos, D	en
dc.contributor.author	Macris, BJ	en
dc.date.accessioned	2014-03-01T01:14:20Z
dc.date.available	2014-03-01T01:14:20Z
dc.date.issued	1999	en
dc.identifier.issn	1389-1723	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/13003
dc.subject	Rhodotorula glutinis	en
dc.subject	lipase production	en
dc.subject	whole cell biocatalyst	en
dc.subject	esterification	en
dc.subject	organic solvents	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Food Science & Technology	en
dc.subject.other	FATTY-ACID PRODUCTION	en
dc.subject.other	EXTRACELLULAR LIPASE	en
dc.subject.other	ASPERGILLUS-NIGER	en
dc.subject.other	PURIFICATION	en
dc.subject.other	ENZYMES	en
dc.title	A novel lipolytic activity of Rhodotorula glutinis cells: Production, partial characterization and application in the synthesis of esters	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/S1389-1723(99)80175-3	en
heal.identifier.secondary	http://dx.doi.org/10.1016/S1389-1723(99)80175-3	en
heal.language	English	en
heal.publicationDate	1999	en
heal.abstract	Cell-bound lipase activity (10 pNPL units/g dry cell weight) was released when the yeast Rhodotorula glutinis was cultured in a 7-l stirred tank fermenter using palm-oil as the sole carbon source. The enzyme showed relative specificity towards medium chain organic acids since the apparent K-m values for pNPB (p-NitroPhenyl-Butyrate) and pNPL (p-NitroPhenyl-Laurate) mere equal to 2.7 and 0.7 mM, respectively. In addition, 80% of this activity could be detected on the surface of the cells. The cell-bound nature of the enzyme increased its thermal stability showing half-life times of 200 and 60 min at 50 and 60 degrees C, respectively, as well as good stability in organic solvents. Freeze-dried cell preparations were successfully used to catalyze the synthesis of fatty acid esters of butanol and heptanol in nearly anhydrous organic solvents. A conversion of 60-62% was obtained upon esterification of palmitic or oleic acid with butanol, within 96 h. The enzyme preparation was used in four consecutive batch reactions with only 10% loss of activity.	en
heal.publisher	SOC BIOSCIENCE BIOENGINEERING JAPAN	en
heal.journalName	JOURNAL OF BIOSCIENCE AND BIOENGINEERING	en
dc.identifier.doi	10.1016/S1389-1723(99)80175-3	en
dc.identifier.isi	ISI:000082763100010	en
dc.identifier.volume	88	en
dc.identifier.issue	1	en
dc.identifier.spage	53	en
dc.identifier.epage	56	en