6UNV

Crystal structure of a methanol tolerant lipase/esterase from the fungus Rasamsonia emersonii

6UNV の概要

• エントリーDOI: 10.2210/pdb6unv/pdb
• 分子名称: Lipase (1 entity in total)
• 機能のキーワード: lipase, esterase, macaw oil hydrolysis, methanol tolerant, hydrolase
• 由来する生物種: Rasamsonia emersonii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31777.69

構造登録者

Vieira, P.S.,Milan, N.,Murakami, M.T.,Zanphorlin, L.M. (登録日: 2019-10-13, 公開日: 2020-06-03, 最終更新日: 2024-11-20)

主引用文献

Rade, L.L.,da Silva, M.N.P.,Vieira, P.S.,Milan, N.,de Souza, C.M.,de Melo, R.R.,Klein, B.C.,Bonomi, A.,de Castro, H.F.,Murakami, M.T.,Zanphorlin, L.M.
A Novel Fungal Lipase With Methanol Tolerance and Preference for Macaw Palm Oil.
Front Bioeng Biotechnol, 8:304-304, 2020

PubMed Abstract: Macaw palm is a highly oil-producing plant, which presents high contents of free fatty acids, being a promising feedstock for biofuel production. The current chemical routes are costly and complex, involving highly harsh industrial conditions. Enzymatic processing is a potential alternative; however, it is hampered by the scarce knowledge on biocatalysts adapted to this acidic feedstock. This work describes a novel lipase isolated from the thermophilic fungus (Lip), which tolerates extreme conditions such as the presence of methanol, high temperatures, and acidic medium. Among the tested feedstocks, the enzyme showed the highest preference for macaw palm oil, producing a hydrolyzate with a final free fatty acid content of 92%. Crystallographic studies revealed a closed conformation of the helical amphipathic that typically undergoes conformational changes in a mechanism of interfacial activation. Such conformation of the is stabilized by a salt bridge, not observed in other structurally characterized homologs, which is likely involved in the tolerance to organic solvents. Moreover, the lack of conservation of the aromatic cluster IxxWxxxxxF in the of Lip with the natural mutation of the phenylalanine by an alanine might be correlated with the preference of short acyl chains, although preserving catalytic activity on insoluble substrates. In addition, the presence of five acidic amino acids in the of Lip, a rare property reported in other lipases, may have contributed to its ability to tolerate and be effective in acidic environments. Therefore, our work describes a new fungal biocatalyst capable of efficiently hydrolyzing macaw oil, an attractive feedstock for the production of "drop-in" biofuels, with high desirable feature for industrial conditions such as thermal and methanol tolerance, and optimum acidic pH. Moreover, the crystallographic structure was elucidated, providing a structural basis for the enzyme substrate preference and tolerance to organic solvents.

PubMed: 32435636
DOI: 10.3389/fbioe.2020.00304

実験手法

X-RAY DIFFRACTION (3 Å)