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Biol Bull 137: 265-276. (October 1969)
© 1969 Marine Biological Laboratory
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STUDIES ON A TREHALASE FROM A SYMBIONT OF THE TROPICAL COCKROACH, BLABERUS CRANIIFER—A SUGGESTED ANALYTICAL ENZYME

FRANK M. FISHER JR. 1 and ROBERT O. McALISTER 1

1 Department of Biology, Rice University, Houston, Texas 77001

1. A trehalase from a gram negative symbiont of Blaberus craniifer has been isolated and purified 80 fold.

2. Hydrolysis of trehalose was linear with respect to time and protein concentration.

3. The pH optimum of the enzyme was found to be 4.6, the Km 2.2 x l0-3 M and the Vmax about 290 µMole trehalose hydrolyzed/mgm protein hr-1.

4. The energy of activation is found to be 9321 Cal/mole and enzymatic hydrolysis was inhibited by monovalent and divalent metal; however, no effect of the sulfhydryl inhibitor PCMB was noted.

5. The merit of this source and this trehalase as an analytic reagent is discussed.






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