NOVELTY - New recombinant lipase/acyltransferase enzyme (A) comprises: only limited amino acid sequence identity to Candida albicans (Cal-L) lipase/acyltransferase, and comprises first pentapeptide sequence motif having specific sequence at residues corresponding to positions 192-196 of specific Candida parasilopsis (Cpa-L) lipases/acyltransferases sequence; second amino acid sequence motif having specific pentapeptide sequence at residues corresponding to positions 210-214 of the Cpa-L lipases/acyltransferases sequence; and lipase/esterase activity.    USE - For forming a detergent composition; for removing oily soil or stain from surface (preferably textile surface); for forming peracid; for forming ester surfactant; and for making biodiesel (claimed). The peracid is e.g. peracetic acid. Also useful for forming perfumes and fragrances; for degumming of vegetable oil; and in molecular biology applications to acylate proteins and nucleic acids, to acylate molecules in making pharmaceutical compounds, and in other reactions where the transfer of an acyl group is desirable.    ADVANTAGE - The recombinant lipase/acyltransferase enzyme provides a novel Candida albicans (CalA)-related lipases/acyl transferases (CALA), which are a family of eukaryotic and prokaryotic lipases/acyltransferases that share limited homology (e.g. about 18-49%) to known extracellular acyltransferases isolated from Candida parasilopsis (Cpa-L) and Cal-L. As evidence of their unknown function, the amino acid sequences now identified as CALA were previously annotated as undefined or were poorly characterized hypothetical proteins that were either not known to be lipases and/or acyltransferases, or were suspected to be lipases but had no known acyltransferase activity.    DETAILED DESCRIPTION - New recombinant lipase/acyltransferase enzyme (A) comprises: only limited amino acid sequence identity to Candida albicans (Cal-L) lipase/acyltransferase, and comprises a first amino acid sequence motif having a sequence of Gly-X1-Ser-X2-Gly at residues corresponding to positions 192-196 of the Candida parasilopsis (Cpa-L) lipase/acyltransferase having a defined amino acid sequence containing 408 amino acids (SEQ ID NO: 8) as given in the specification; a second amino acid sequence motif having a sequence of Tyr-Ala-X1a-X2a-X3a at residues corresponding to positions 210-214 of the Cpa-L lipase/acyltransferase amino acid sequence (SEQ ID NO: 8); and lipase/esterase activity based on hydrolysis of para-nitrophenylbutyrate in an aqueous solution.    X1=aromatic amino acid;    X2=amino acid selected from Gly, Glu, or Gln;    X1a=Pro, or Lys    X2a=acidic amino acid;    X3a=non-polar aliphatic amino acid.    INDEPENDENT CLAIMS are included for the following:    (1) a composition (C1) comprising: the lipase/acyltransferase enzyme (A);    (2) method (M1) for removing an oily soil or stain from a surface involving: contacting the surface with the composition (C1);    (3) method (M2) for forming a peracid involving: contacting an acyl donor and hydrogen peroxide with the lipase/acyltransferase enzyme (A);    (4) method (M3) for forming an ester surfactant involving: contacting an acyl donor and acceptor with the lipase/acyltransferase enzyme (A);    (5) method (M4) for making biodiesel involving: contacting an acyl donor and acceptor with the lipase/acyltransferase enzyme (A);    (6) an expression vector (V1) comprising: a polynucleotide encoding the lipase/acyltransferase enzyme (A) and a signal sequence to cause secretion of the lipase/acyltransferase enzyme;    (7) an expression vector (V2) comprising: a polynucleotide encoding the lipase/acyltransferase enzyme (A') from Cal-L or Cpa-L and a signal sequence to cause secretion of the lipase/acyltransferase enzyme;    (8) method (M5) for producing the lipase/acyltransferase enzyme (A); and    (9) method (M6) for expressing the lipase/acyltransferase enzyme (A') involving: introducing the expression vector (V2) into a host, expressing the lipase/acyltransferase enzyme, and recovering the lipase/acyltransferase enzyme expressed.