Kinetic characteristics of the alpha-mannanase of Rhodococcus erythropolis 19
Pavlova, I.N.; Tamm, V.E.
Mikrobiolohichnyi Zhurnal 49(2): 11-15
1987
ISSN/ISBN: 0201-8462 PMID: 3508931 Document Number: 300377
Being subjected to the submerged cultivation on the medium containing cells of baker's yeast as a carbon source Rhodococcus erythropolis 19 synthesizes the extracellular .alpha.-mannanase which hydrolyzes .alpha.-1.2 and .alpha.-1.3-bonds in the mannan molecule according to the exotype. Km for mannan of baker's yeast is equal to 0.27 mg/ml and the maximal reaction rate (Vmax) is 0.69 .mu.mol/min. The enzyme is inhibited by EDTA and reagents for SH-groups. The inhibition constant (Ki) of the mannanase reaction is 5.59 .cntdot. 10-5 M for EDTA and 3.0 .cntdot.10-4 M for p-chloromercury-benzoate.