You have an enzymatic reaction proceeding at the optimum ph and optimum temperature. you add a competitive inhibitor to the reaction and notice that the reaction slows down.

what can you do to speed the reaction up again?

add more inhibitor to speed up the reaction.
add more substrate; it will outcompete the inhibitor and increase the reaction rate.
increase the temperature.
increase the ph.

Add more substrate.

Explanation:

First let's explain why all the other options are wrong:

A competitive inhibitor is a substance that resembles the substrate that normally reacts with the enzime, so it binds to the enzime's active sites and prevents the substrate from doing so. Adding more substrate makes it more likely than a substrate molecule binds to an enzime's active site instead of the inhibitor ("it will outcompete the inhibitor and increase the reaction rate").

a saline water is fed to a reverse osmosis unit at flow rate o rotameter connected to reject (retentate) line reads 8 installed in reject and permeate line reads 15.2 milli siemens/cm and 300 micro siemens/com respectively.

catya your not at all which answer i've seen you do this on another question!