A huge amount of phospholipids or lecithin is produced as a byproduct in the vegetable oil industry. However, most are just used as a feed additive. This study has focused on enzymatic valorization of lecithin. This was exploited by enzymatic transformation of soy lecithin into lysolecithin liposomes, including functional free fatty acids, hydroxy fatty acids, hydrocarbons, or secondary fatty alcohols. One of the representative examples was the preparation of lysolecithin liposomes containing secondary fatty alcohols [e.g., 9-Hydroxyheptadec-11-ene (9) and 9-heptadecanol (10)] by using a phospholipase A2 from Streptomyces violaceoruber, a fatty acid double-bond hydratase from Stenotrophomonas maltophilia, and a photoactivated decarboxylase from Chlorella variabilis NC64A. The engineered liposomes turned out to range ca. 144 nm in diameter by dynamic light scattering analysis. Thereby, this study will contribute to application of functional fatty acids and their derivatives as well as valorization of lecithin for the food and cosmetic industries.

Secretory phospholipase A2 (sPLA2), which hydrolyzes the sn-2 acyl bond of lecithin in a Ca2+-dependent manner, is an important enzyme in the oil and oleochemical industries. However, most sPLA2s are not stable under process conditions. Therefore, a thermostable sPLA2 was investigated in this study. A marine bacterial sPLA2 isolated from Sciscionella marina (Sm-sPLA2) was catalytically active even after 5 h of incubation at high temperatures of up to 50°C, which is outstanding compared with a representative bacterial sPLA2 (i.e. sPLA2 from Streptomyces violaceoruber; Sv-sPLA2). Consistent with this, the melting temperature of Sm-sPLA2 was measured to be 7.7°C higher than that of Sv-sPLA2. Furthermore, Sm-sPLA2 exhibited an improved biotransformation performance compared with Sv-sPLA2 in the hydrolysis of soy lecithin to lysolecithin and free fatty acids at 50°C. Structural and mutagenesis studies revealed that the Trp41-mediated anchoring of a Ca2+-binding loop into the rest of the protein body is directly linked to the thermal stability of Sm-sPLA2. This finding provides a novel structural insight into the thermostability of sPLA2 and could be applied to create mutant proteins with enhanced industrial potential.