ArticleFrontiers in microbiology2026
Screening of mutants, enzymatic properties, and scale-up fermentation for catalysis of naringin using recombinant
Article in Frontiers in microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: Prunin is scarce in nature and suffers from low extraction efficiency, and industrial-scale production of prunin and L-rhamnose remains technically inadequate. Therefore, developing an Methods: An Results: The purified recombinant enzyme (120.7 kDa) showed optimal activity at 75 °C and pH 5.0, with a Km of 5.23 mM toward pNPR. A key mutant, R11, exhibited 22.2% higher relative activity than the wild type. After tank fermentation, enzyme activities of both wild-type and R11 were increased approximately two-fold, and the conversion rate of naringin to prunin by R11 was 2.77-fold higher than that of the unoptimized wild-type control. Conclusion: The recombinant
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