TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preferred Enzyme: The lipase/acyltransferase enzyme has less than 50% amino acid sequence identity to Cal-L lipase/acyltransferase having the amino acid sequence (SEQ ID NO: 8); and has a precursor amino acid sequence of greater than or equal to 390 amino acid residues. The first amino acid sequence motif has a sequence selected from Gly-Tyr-Ser-Gly-Gly, Gly-Tyr-Ser-Gln-Gly, and Gly-His-Ser-Gln-Gly. The second amino acid sequence motif has a sequence selected from Tyr-Ala-Pro-Glu-Leu, Tyr-Ala-Pro-Asp-Val, Tyr-Ala-Pro-Asp-Leu, Tyr-Ala-Pro-Glu-Ile, and Tyr-Ala-Lys-Glu-Leu. The lipase/acyltransferase enzyme of has an amino acid sequence having greater than or equal to 90% identity to an amino acid sequence selected from 16 amino acid sequences as given in the specification e.g. polypeptides having defined amino acid sequences containing 231 (SEQ ID NO: 2), 482 (SEQ ID NO: 11), 387 (SEQ ID NO: 14), 418 (SEQ ID NO: 17), or 394 (SEQ ID NO: 20) amino acids as given in the specification. The lipase/acyltransferase enzyme does not have the amino acid sequence containing 444 (SEQ ID NO: 5), or 448 (SEQ ID NO: 8) amino acids as given in the specification. The lipase/acyltransferase enzyme is selected from Arxula adeninovirans (Aad-L), Pichia stiptis (Pst-L), Streptomyces coelicolor (Sco-L), Malassezia furfur (Mfu-L), Rhodococcus sp. (Rsp-L), Corynebacterium jeikeium (Cje-L), Ate-L, Aor-L-0488, Afu-L, Ani-L, Acl-L, Aor-L-6767, Fve-L, Fgr-L, Ksp-L, and Dha-L; provided that the lipase/acyltransferase enzyme is not Cal-L or Cpa-L. In the composition (C1) and the method (M1) to (M4), the lipase/acyltransferase enzyme is expressed in a heterologous host cell. The composition (C1) is a detergent composition, and the lipase/acyltransferase enzyme is Sco-L. In the method (M2), the lipase/acyltransferase enzyme used is Aad-L. In the method (M3), the lipase/acyltransferase enzyme used is Aad-L, Pst-L, Sco-L, or Mfu-L. In the method (M4), the lipase/acyl transferase enzyme used is Aad-L, or Pst-L. Recombinant Methods (claimed): The method (M5) for expressing the lipase/acyltransferase enzyme (A) involves: introducing the expression vector (V1) into a host, expressing the lipase/acyltransferase enzyme, and recovering the lipase/acyltransferase enzyme (A) expressed. Preferred Definitions:    X1=Tyr, or His;    X2=Gly, or Gln;    X2a=Asp, or Glu;    X3a=Leu, Val, or Ile.    EXAMPLE - The recombinant lipase/acyltransferase enzyme form Arxula adeninovirans (Aad-L) and Pichia stiptis (Pst-L), were evaluated for ability to generate biodiesel, by evaluating their ability to perform a synthetic reaction using triolein as the acyl donor and methanol or ethanol as the acyl acceptor. For assaying activity, triolein in 4% gum arabic emulsion (20 mu l, 20 g/L) was added to 50 mM phosphate buffer at pH 6 or 8 in 96-well microtiter plates. Acceptor (methanol or ethanol) (8 vol./vol.%) was added to each well. Appropriately diluted enzyme solution was added to the wells and the plate was incubated overnight at 30 degrees C, with continuous mixing. After incubation, the supernatant (100 mu l) was added to acetone (900 mu l) in a microfuge tube and the contents were spun in a microcentrifuge. After centrifugation, the supernantant was transferred to a fresh tube and further diluted 3-fold with acetone, and this diluted supernatant (30 mu l) was analyzed by liquid chromatography/mass spectroscopy (LC/MS) charged aerosol detection (CAD) analysis, by using Agilent 1100 (RTM: HPLC) was equipped with Alltima HP C18 (RTM: column). It was observed that biodiesel consisting of fatty acid methyl and ethyl esters were formed.