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Publication Abstract from PubMed

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

Structural and functional characterization of a thermostable secretory phospholipase A(2) from Sciscionella marina and its application in liposome biotransformation.,Kang BG, Kwon SY, Lee HR, Hwang Y, Youn SY, Oh C, Park JB, Cha SS Acta Crystallogr D Struct Biol. 2023 Feb 1;79(Pt 2):188-197. doi: , 10.1107/S2059798323000384. Epub 2023 Feb 6. PMID:36762864^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.