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Investigation of Structural Features of Two Related Lipases and the Impact on Fatty Acid Specificity in Vegetable Fats

Dong, Zehui LU ; Olofsson, Kim ; Linares-Pastén, Javier A. LU orcid and Nordberg Karlsson, Eva LU orcid (2022) In International Journal of Molecular Sciences 23(13).
Abstract
One of the indispensable applications of lipases in modification of oils and fats is the possibility to tailor the fatty acid content of triacylglycerols (TAGs), to meet specific requirements from various applications in food, nutrition, and cosmetic industries. Oleic acid (C18:1) and stearic acid (C18:0) are two common long fatty acids in the side chain of triglycerides in plant fats and oils that have similar chemical composition and structures, except for an unsaturated bond between C9 and C10 in oleic acid. Two lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL), show activity in reactions involving oleate and stearate, and share high sequence and structural identity. In this research, the preference for one of these two... (More)
One of the indispensable applications of lipases in modification of oils and fats is the possibility to tailor the fatty acid content of triacylglycerols (TAGs), to meet specific requirements from various applications in food, nutrition, and cosmetic industries. Oleic acid (C18:1) and stearic acid (C18:0) are two common long fatty acids in the side chain of triglycerides in plant fats and oils that have similar chemical composition and structures, except for an unsaturated bond between C9 and C10 in oleic acid. Two lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL), show activity in reactions involving oleate and stearate, and share high sequence and structural identity. In this research, the preference for one of these two similar fatty acid side chains was investigated for the two lipases and was related to the respective enzyme structure. From transesterification reactions with 1:1 (molar ratio) mixed ethyl stearate (ES) and ethyl oleate (EO), both RML and ROL showed a higher activity towards EO than ES, but RML showed around 10% higher preference for ES compared with ROL. In silico results showed that stearate has a less stable interaction with the substrate binding crevice in both RML and ROL and higher tendency to freely move out of the substrate binding region, compared with oleate whose structure is more rigid due to the existence of the double bond. However, Trp88 from RML which is an Ala at the identical position in ROL shows a significant stabilization effect in the substrate interaction in RML, especially with stearate as a ligand. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Fungal Proteins/chemistry, Lipase/chemistry, Molecular Docking Simulation, Oleic Acids, Rhizomucor/enzymology, Rhizopus oryzae/enzymology, Sequence Analysis, Protein, Stearates, Structure-Activity Relationship, Substrate Specificity
in
International Journal of Molecular Sciences
volume
23
issue
13
article number
7072
publisher
MDPI AG
external identifiers
  • pmid:35806072
  • scopus:85132701870
ISSN
1422-0067
DOI
10.3390/ijms23137072
language
English
LU publication?
yes
id
bc12f6d3-e13c-4fa2-a3c4-1518d1929674
date added to LUP
2022-06-27 23:16:18
date last changed
2024-04-16 09:26:23
@article{bc12f6d3-e13c-4fa2-a3c4-1518d1929674,
  abstract     = {{One of the indispensable applications of lipases in modification of oils and fats is the possibility to tailor the fatty acid content of triacylglycerols (TAGs), to meet specific requirements from various applications in food, nutrition, and cosmetic industries. Oleic acid (C18:1) and stearic acid (C18:0) are two common long fatty acids in the side chain of triglycerides in plant fats and oils that have similar chemical composition and structures, except for an unsaturated bond between C9 and C10 in oleic acid. Two lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL), show activity in reactions involving oleate and stearate, and share high sequence and structural identity. In this research, the preference for one of these two similar fatty acid side chains was investigated for the two lipases and was related to the respective enzyme structure. From transesterification reactions with 1:1 (molar ratio) mixed ethyl stearate (ES) and ethyl oleate (EO), both RML and ROL showed a higher activity towards EO than ES, but RML showed around 10% higher preference for ES compared with ROL. In silico results showed that stearate has a less stable interaction with the substrate binding crevice in both RML and ROL and higher tendency to freely move out of the substrate binding region, compared with oleate whose structure is more rigid due to the existence of the double bond. However, Trp88 from RML which is an Ala at the identical position in ROL shows a significant stabilization effect in the substrate interaction in RML, especially with stearate as a ligand.}},
  author       = {{Dong, Zehui and Olofsson, Kim and Linares-Pastén, Javier A. and Nordberg Karlsson, Eva}},
  issn         = {{1422-0067}},
  keywords     = {{Fungal Proteins/chemistry; Lipase/chemistry; Molecular Docking Simulation; Oleic Acids; Rhizomucor/enzymology; Rhizopus oryzae/enzymology; Sequence Analysis, Protein; Stearates; Structure-Activity Relationship; Substrate Specificity}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{13}},
  publisher    = {{MDPI AG}},
  series       = {{International Journal of Molecular Sciences}},
  title        = {{Investigation of Structural Features of Two Related Lipases and the Impact on Fatty Acid Specificity in Vegetable Fats}},
  url          = {{http://dx.doi.org/10.3390/ijms23137072}},
  doi          = {{10.3390/ijms23137072}},
  volume       = {{23}},
  year         = {{2022}},
}