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Effects of Lipase Immobilization Conditions and Support Materials for the Production of Structured Triacylglycerols

Causevic, Ariana LU ; Olofsson, Kim LU ; Adlercreutz, Patrick LU orcid and Grey, Carl LU (2023) In European Journal of Lipid Science and Technology 125(2).
Abstract

Structured triacylglycerols (STAG) with desired properties can be synthesized by transesterification using immobilized lipases. Herein, the effect of immobilization conditions and support material on the immobilization yield, specific activity and regioselectivity of lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL) in the production of STAG, are evaluated. Four different support materials utilizing adsorption and one with covalent binding are investigated. Ammonium sulfate is found to significantly increase the activity-based immobilization yield (12% and 38% for RML and ROL, respectively) and specific activity on Accurel MP1000 (MP1000) when used as the immobilization buffer. Furthermore, the immobilization principle and... (More)

Structured triacylglycerols (STAG) with desired properties can be synthesized by transesterification using immobilized lipases. Herein, the effect of immobilization conditions and support material on the immobilization yield, specific activity and regioselectivity of lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL) in the production of STAG, are evaluated. Four different support materials utilizing adsorption and one with covalent binding are investigated. Ammonium sulfate is found to significantly increase the activity-based immobilization yield (12% and 38% for RML and ROL, respectively) and specific activity on Accurel MP1000 (MP1000) when used as the immobilization buffer. Furthermore, the immobilization principle and support material influenced both the activity and regiospecificity. Immobilization by adsorption is found to result in higher catalytic activity, while covalent binding resulted in lipase inactivation. For RML, the highest specific activity of 43 µmol STAG min−1 g−1 (U) is obtained on MP1000, while ROL, which exhibited higher activities in general, results in a maximum activity of 120 U on Lifetech ECR8806. The obtained specific activites are comparable to the commercial preparations Novozym 40086 (45 U) and Lipase DF “Amano” IM (147 U) while the regiospecificity of the developed preparations is even higher, forming at least 64% less byproduct. Practical applications: There is an increasing need for lipids with specific nutritional and physical properties in health, nutrition, and food applications. In this context, STAG are highly promising products due to the possibility to tailor the composition to obtain the desired properties. Immobilized lipases are the catalyst of choice for the production of STAG, in which activity and regioselectivity are particularly important parameters for the process performance. In this study, it is shown that these parameters can be affected by the immobilization conditions and support material. Immobilized preparations with high activity and excellent regiospecificity are created on commercially available supports. This shows the possibility of STAG synthesis with high purity and beneficial properties.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
adsorptions, covalent binding, enzymatic transesterification, lipase immobilization, structured triacylglycerol
in
European Journal of Lipid Science and Technology
volume
125
issue
2
article number
2200135
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:85147420339
ISSN
1438-7697
DOI
10.1002/ejlt.202200135
language
English
LU publication?
yes
id
30b5c821-434b-41de-82f0-41321f5fa3e5
date added to LUP
2023-02-21 15:24:15
date last changed
2023-08-16 09:38:22
@article{30b5c821-434b-41de-82f0-41321f5fa3e5,
  abstract     = {{<p>Structured triacylglycerols (STAG) with desired properties can be synthesized by transesterification using immobilized lipases. Herein, the effect of immobilization conditions and support material on the immobilization yield, specific activity and regioselectivity of lipases from Rhizomucor miehei (RML) and Rhizopus oryzae (ROL) in the production of STAG, are evaluated. Four different support materials utilizing adsorption and one with covalent binding are investigated. Ammonium sulfate is found to significantly increase the activity-based immobilization yield (12% and 38% for RML and ROL, respectively) and specific activity on Accurel MP1000 (MP1000) when used as the immobilization buffer. Furthermore, the immobilization principle and support material influenced both the activity and regiospecificity. Immobilization by adsorption is found to result in higher catalytic activity, while covalent binding resulted in lipase inactivation. For RML, the highest specific activity of 43 µmol STAG min<sup>−1</sup> g<sup>−1</sup> (U) is obtained on MP1000, while ROL, which exhibited higher activities in general, results in a maximum activity of 120 U on Lifetech ECR8806. The obtained specific activites are comparable to the commercial preparations Novozym 40086 (45 U) and Lipase DF “Amano” IM (147 U) while the regiospecificity of the developed preparations is even higher, forming at least 64% less byproduct. Practical applications: There is an increasing need for lipids with specific nutritional and physical properties in health, nutrition, and food applications. In this context, STAG are highly promising products due to the possibility to tailor the composition to obtain the desired properties. Immobilized lipases are the catalyst of choice for the production of STAG, in which activity and regioselectivity are particularly important parameters for the process performance. In this study, it is shown that these parameters can be affected by the immobilization conditions and support material. Immobilized preparations with high activity and excellent regiospecificity are created on commercially available supports. This shows the possibility of STAG synthesis with high purity and beneficial properties.</p>}},
  author       = {{Causevic, Ariana and Olofsson, Kim and Adlercreutz, Patrick and Grey, Carl}},
  issn         = {{1438-7697}},
  keywords     = {{adsorptions; covalent binding; enzymatic transesterification; lipase immobilization; structured triacylglycerol}},
  language     = {{eng}},
  number       = {{2}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{European Journal of Lipid Science and Technology}},
  title        = {{Effects of Lipase Immobilization Conditions and Support Materials for the Production of Structured Triacylglycerols}},
  url          = {{http://dx.doi.org/10.1002/ejlt.202200135}},
  doi          = {{10.1002/ejlt.202200135}},
  volume       = {{125}},
  year         = {{2023}},
}