Abstract:
:A novel strain of Rhizopus oryzae WPG secretes a noninduced lipase (ROLw) in the culture medium; purified ROLw is a protein of 29 kDa, the 45 N-terminal amino acid residues were sequenced, this sequence is very homologous to Rhizopus delemar lipase (RDL), Rhizopus niveus lipase (RNL) and R. oryzae lipase (ROL29) sequences; the cloning and sequencing of the part of the gene encoding the mature ROLw, shows two nucleotides differences with RDL, RNL and ROL29 sequences corresponding to the change of the residues 134 and 200; ROLw does not present the interfacial activation phenomenon when using tripropionin or vinyl propionate as substrates; the lipase activity is maximal at pH 8 and at 37 degrees C, specific activities of 3500 or 900 U mg(-1) were measured at 37 degrees C and at pH 8, using olive oil emulsion or tributyrin as substrates, respectively; ROLw is unable to hydrolyse triacylglycerols in the presence of high concentration of bile salts; it is a serine enzyme as it is inhibited by tetrahydrolipstatin and was stable between pH 5 and pH 8.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Salah RB,Mosbah H,Fendri A,Gargouri A,Gargouri Y,Mejdoub Hdoi
10.1111/j.1574-6968.2006.00323.xsubject
Has Abstractpub_date
2006-07-01 00:00:00pages
241-8issue
2eissn
0378-1097issn
1574-6968pii
FML323journal_volume
260pub_type
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