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Galactose to tagatose isomerization at moderate temperatures with high conversion and productivity.


ABSTRACT: There are many industrially-relevant enzymes that while active, are severely limited by thermodynamic, kinetic, or stability issues (isomerases, lyases, transglycosidases). In this work, we study Lactobacillus sakei L-arabinose isomerase (LsLAI) for D-galactose to D-tagatose isomerization-that is limited by all three reaction parameters. The enzyme demonstrates low catalytic efficiency, low thermostability at temperatures > 40 °C, and equilibrium conversion < 50%. After exploring several strategies to overcome these limitations, we show that encapsulating LsLAI in gram-positive Lactobacillus plantarum that is chemically permeabilized enables reactions at high rates, high conversions, and elevated temperatures. In a batch process, this system enables ~ 50% conversion in 4 h starting with 300 mM galactose (an average productivity of 37 mM h-1), and 85% conversion in 48 h. We suggest that such an approach may be invaluable for other enzymatic processes that are similarly kinetically-, thermodynamically-, and/or stability-limited.

SUBMITTER: Bober JR 

PROVIDER: S-EPMC6779876 | biostudies-other | 2019 Oct

REPOSITORIES: biostudies-other

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Galactose to tagatose isomerization at moderate temperatures with high conversion and productivity.

Bober Josef R JR   Nair Nikhil U NU  

Nature communications 20191007 1


There are many industrially-relevant enzymes that while active, are severely limited by thermodynamic, kinetic, or stability issues (isomerases, lyases, transglycosidases). In this work, we study Lactobacillus sakei L-arabinose isomerase (LsLAI) for D-galactose to D-tagatose isomerization-that is limited by all three reaction parameters. The enzyme demonstrates low catalytic efficiency, low thermostability at temperatures > 40 °C, and equilibrium conversion < 50%. After exploring several strateg  ...[more]

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