4.7 Article

An Electrospun Sandwich-Type Lipase-Membrane Bioreactor for Hydrolysis at Macroscopic Oil-Water Interfaces

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 70, Issue 2, Pages 584-591

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.1c04042

Keywords

lipase; electrospinning; membrane bioreactor; macroscopic interface

Funding

  1. National Natural Science Foundation of China [31972015]
  2. Support Project of High-level Teachers in Beijing Municipal Uni-versities in the Period of the 13th Five-year Plan [CITTCD201904039]
  3. General Projects of Beijing Municipal Education Commission [KM202010011008]
  4. Graduate Innovation Project of School of Food and Health in 2021

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The core task of designing lipase catalytic systems is to create a suitable oil-water interface for lipase distribution. In this study, sandwich-type lipase-membrane bioreactors (SLMBs) were fabricated using a layer-by-layer electrospinning process. These SLMBs demonstrated improved catalytic efficiency compared to free lipase, as well as better pH adaptability, temperature resistance, storage stability, and reusability.
The core task for lipase catalytic system design is to construct a suitable oil-water interface for lipase distribution. In comparison to the micro-oil-water interface, the macro-oil-water interface (top oil-bottom water) served as a simplified lipase catalytic system that is more in line with industrial applications but limited in catalytic efficiency. Based on the assumption that one potential carrier can help lipase reach to the macro-oil-water interface, in the current work, sandwich-type lipase-membrane bioreactors (SLMBs) fabricated by a facile layer-by-layer electrospinning process were reported. These SLMBs were composed of a hydrophilic polyamide 6 nanofibrous membrane (NFM) as the bottom layer, a blended electrospun lipase/PVA NFM as the middle layer, and a hydrophobic EC/PU NFM as the top layer. The lipase loading can be controlled by altering the electrospinning time of the middle layer. Under the optimized conditions, the catalytic efficiency of the SLMBs was 2.05 times higher than that of free lipase. In addition, the SLMBs exhibit much better pH (high activity over a broad pH range of 5-10), temperature (retained 62% at 80 degrees C), storage stability (no loss of activity after being stored at 4 degrees C for 11 days), and reusability (retained 23% after five cycles) than free lipase.

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