TECHNOLOGY FOCUS - BIOLOGY - Preferred Components: The sn-1,3 positional specific lipase is T. lanuginose, Rhizomucor miehei, Mucor miehei, Pseudomonas sp., Rhizopus sp. (preferably R. niveus or R. oryzae), Mucor javanicus, Aspergillus niger (all preferred), Penicillium roqueforti, Acromobacter sp. or Burkholderia sp., and the lipase having increased affinity for partial glycerides is C. antarctica B, Candida rugosa, Alcaligenes sp. or Penicillium camembertii.    TECHNOLOGY FOCUS - ORGANIC CHEMISTRY - Preferred Components: The fatty acid source comprises at least one or two of soybean oil, canola oil, rapeseed oil, olive oil, castor oil, palm oil, sunflower oil, peanut oil, cotton seed oil, Jatropha oil, animal-derived fat, waste cooking oil, or oil triglycerides derived from inedible plant sources. The lipases are jointly immobilized on the suitable support, where the supports on which the lipases are immobilized are identical or different. The support is a porous support, which is organic or inorganic, where the inorganic porous support is silica-based or alumina-based, and the organic porous support is polymer-based, and the support optionally contains active functional groups of epoxy and aldehyde groups or ionic groups. Preferred Process: The conversion of the fatty acid acyl groups or free fatty acids comprised in the fatty acid source to fatty acid methyl esters is monitored at various time points during the reaction, the reaction medium is removed by suitable means at any desired time point during the reaction, thus stopping the reaction, and the formed fatty acid methyl esters and the optionally formed glycerol are isolated from the reaction medium. The reaction is stopped when the conversion of the fatty acid acyl groups or free fatty acids comprised in the fatty acid source to fatty acid methyl esters has reached at least 70%. In the process, the lipase preparation comprises one single lipase immobilized on a suitable support, or a mixture of at least two lipases jointly or separately immobilized on the suitable support. The process allows the reaction to proceed until the conversion of the fatty acid acyl groups or free fatty acids comprised in the fatty acid source to fatty acid methyl esters reaches at least 70%, while continuously removing the formed glycerol from the reaction mixture, to yield an organic phase containing mainly residual unreacted glycerides and the formed fatty acid alkyl esters; and comprises the step of reacting the organic phase with the short-chain free alcohol in the presence of the lipase preparation until the conversion of the fatty acid acyl groups or free fatty acids to fatty acid methyl esters reaches at least 85% or 95%. The insoluble support is Amberlite XAD-1600 (RTM: Adsorbent resin) or Amberlite 7HP (RTM: Adsorbent resin). The solvent is n-hexane. The lipase preparation comprises first and second lipases, where the first lipase exhibits higher transesterification activity towards triglycerides compared to its activity towards partial glycerides, and the second lipase exhibits higher transesterification activity towards partial glycerides compared to its activity towards triglycerides. The first lipase releases intermediates in a first transesterification reaction, which are favored by the second lipase for transesterification with an alcohol to form fatty acid alkyl esters. The lipases exhibit different substrate specificities that maintain their transesterification activity to triglycerides when used together, while at least one of the two lipases decays in the transesterification reaction medium when used separately with triglycerides as substrate but exhibits high transesterification activity with partial glycerides as substrate. EXAMPLE - Lipase derived from Thermomyces lanuginosa (1 ml) was solubilized in a Tris buffer solution (12 ml) of 0.05M and pH 8. The lipase solution was contacted with an enzyme support e.g. Amberlite XAD-1600 (RTM: Adsorbent resin) (1 g) by shaking or stirring for 8 hours at room temperature. A hydrophobic organic solvent, such as n-hexane, was added to the immobilization medium at a ratio of 1:10-10:1 buffer:organic solvent, respectively. The support containing the immobilized enzyme was filtered off and dried in a desiccator overnight to yield the immobilized lipase. The immobilized lipase (30 g) was added to soybean oil (220 g) and methyl alcohol (23.9 g) into a double-jacketed glass reactor. Methanol was added in batches. The reaction system was mechanically stirred at 30 degrees C to give fatty acid methyl ester.