You might have heard of ginsenoside Rh2, a compound with amazing health benefits. It can help fight certain cancers, reduce inflammation, and even tackle diabetes. But how do we make more of this wonder substance? Scientists have been looking into an enzyme called UGT51 from yeast, which plays a key role in making ginsenoside Rh2. The problem? This enzyme isn't very good at its job.

So, researchers decided to give UGT51 a makeover. They changed four specific parts of the enzyme (E805A, S998A, R1031A, and L1032A). These tweaks made the enzyme more stable, better at binding, and easier for the main ingredient, protopanaxadiol (PPD), to get to its active site.

Under lab conditions, three of these mutated enzymes showed improved activity. The best of the bunch, a double mutant called R1031A/L1032A, had an amazing 85% boost in activity. When they used this in a special process called fed-batch technology, they were able to produce 4. 663 grams of Rh2 per liter.

But how did these changes work? To find out, they used computer simulations to watch how the enzyme moved and behaved. These simulations showed that the structure of the enzyme changed a lot, especially in the R1031A/L1032A version. These changes helped the enzyme do its job better.

This new way of making changes to enzymes could be a big deal. It could help create more efficient enzymes for all sorts of important jobs in the future.

Unlocking the Power of UGT51: A New Way to Produce Rare Ginsenoside Rh2

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