Structural and functional characterization of a thermostable secretory phospholipase A 2 from Sciscionella marina and its application in liposome biotransformation

Bu Gyeong Kang, Seung Yeon Kwon, Hyo Ran Lee, Yeji Hwang, So Yeon Youn, Chulhong Oh, Jin Byung Park, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)188-197
Number of pages10
JournalActa Crystallographica Section D: Structural Biology
Volume79
DOIs
StatePublished - 6 Feb 2023

Bibliographical note

Publisher Copyright:
© 2023 International Union of Crystallography. All rights reserved.

Keywords

  • Sciscionella marina
  • crystal structure
  • liposome biotransformation.
  • loop anchoring
  • phospholipase A2
  • thermostability

Fingerprint

Dive into the research topics of 'Structural and functional characterization of a thermostable secretory phospholipase A 2 from Sciscionella marina and its application in liposome biotransformation'. Together they form a unique fingerprint.

Cite this