Purification and Characterization of Triacylglycerol Lipase fromAspergillus oryzae

Cloning and sequencing of the triacylglycerol lipase gene of Aspergillus oryzae and its expression in Escherichia coli

“…The amino acid sequences of positions 31^55 and 167^195 in Fig. 1 are identical to the determined N-terminal sequence of the mature L3 protein (NAPLNEFLSALLSHLPAIDGTIDAV) [5], and the Nterminal amino acid sequence of a cyanogen bromidecleaved fragment described above, respectively. Therefore, the signal sequence is concluded to be from Met1 to Arg30, which contains a basic amino acid at position 2 and a long hydrophobic region at positions 8^23.…”

“…The cells in the suspension were disrupted by ultrasonication, and then the resultant homogenate was used to assay lipase. Lipase activity was assayed at 30³C for 6 h by the method involving triolein as the substrate, as described previously [5]. The amount of total protein was measured by the method of Lowry et al [9] with bovine serum albumin as the standard.…”

Three Acyltransferases and Nitrogen-responsive Regulator Are Implicated in Nitrogen Starvation-induced Triacylglycerol Accumulation in Chlamydomonas

“…Some of these are annotated as TAG lipases, which would be counterintuitive, but they may well be membrane lipid lipases that release fatty acids that are subsequently incorporated into TAGs. Indeed, a recombinant tomato enzyme showed equal activity on TAG as on phosphatidylcholine, and a putative TAG lipase from Aspergillus oryzae showed activity on mono-and diacylglycerols as well (79,80).…”

Purification and Characterization of Acid Phosphatase from Monocrotophos (MCP) Hydrolyzing Aspergillus niger ITCC 7782.10 Isolated from Local Agricultural Field

“…In addition, the enzyme was completely inhibited by sulfhydryl reagent 2-mercaptoethanol, a well-known thiol group inhibitor, which supports the possibility of involvement of sulfhydryl groups in the catalytic site of the enzyme [17,[24][25][26][27][28][29][30]. The metal-chelating agent EDTA did not inhibit the purified enzyme activity, suggesting the absence of any role of divalent cations for the activation of the enzyme.…”