Abstract
Cell-bound cholinesterase enzyme activity is reported for the first time in the mycelium ofTrichoderma harzianum. This enzyme hydrolyzes both the acetylcholine and the butyryl thiocholine esters. TheK m andV max for choline ester are 0.69 mM and 1.0 nmol acid released min−1 μg−1 protein. However, the thiocholine ester has aK m value of 2.2 mM andV max value of 3.33 nmol product formed min.−1 μg−1 protein. The enzyme is inhibited by eserine, a true classical cholinesterase inhibitor.
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