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Production of high-oleic acid tallow fractions using lipase-catalyzed directed interesterification, using both batch
Enzyme and Microbial Technology
|July 19, 2000
Summary
Immobilized lipases enhance tallow olein unsaturation through enzymatic interesterification. This process yields healthier, low-saturated fat products for food applications, surpassing traditional methods.
Area of Science:
- Biotechnology
- Food Science
- Chemical Engineering
Background:
- Traditional tallow fractionation yields oleins with limited unsaturated fatty acid content.
- Enzymatic interesterification offers a potential route to enhance olein quality.
Purpose of the Study:
- To investigate the use of immobilized lipases for directed interesterification of tallow.
- To compare enzymatic methods with traditional fractionation for producing high-unsaturation oleins.
- To develop a sustainable process for creating healthier tallow-based food ingredients.
Main Methods:
- Utilized immobilized lipase (Novozym 435) in batch and continuous flow reactors for tallow interesterification.
- Controlled reaction conditions, including water activity and temperature, to optimize enzyme activity and product yield.
- Integrated enzymatic interesterification with a crystallization vessel in a continuous flow system.
Main Results:
- Batch interesterification with 2% Novozym 435 increased olein unsaturation to 57% compared to 45% in controls.
- Continuous flow reactor operation produced olein with up to 60% unsaturated fatty acids.
- Enzyme activity was maintained through controlled water activity and could be restored after dehydration.
- Enzyme reusability was demonstrated, with potential enhancement through preincubation.
Conclusions:
- Immobilized lipase-catalyzed interesterification is effective in producing tallow oleins with significantly higher unsaturated fatty acid content.
- The developed continuous flow process offers a basis for industrial production of healthier, low-saturated fat tallow fractions.
- Careful control of water activity is crucial for maintaining enzyme stability and minimizing free fatty acid formation during reuse.
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