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3.2.1.78: mannan endo-1,4-beta-mannosidase

This is an abbreviated version!
For detailed information about mannan endo-1,4-beta-mannosidase, go to the full flat file.

Word Map on EC 3.2.1.78

Reaction

Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
+
H2O
=
Manbeta(1-4)Manbeta(1-4)Man
 +
Manbeta(1-4)Man

Synonyms

(1,4)-beta-D-mannan mannanohydrolase, 1,4-beta-D-mannan mannanohydrolase, 1,4-beta-mannanase, beta-1,4-D-mannanase, beta-1,4-mannan 4-mannanohydrolase, beta-1,4-mannanase, beta-D-mannanase, Beta-mannanase, beta-mannanase B, CaMan, CelB, cold-adapted beta-mannanase, CsMan5, CtManf, Dtur_0671, em26a, endo-1,4-beta-D-mannanase, endo-1,4-beta-mannanase, endo-1,4-mannanase, endo-acting beta-1,4-mannanase, endo-beta 1,4-mannanase, endo-beta-(1,4)-mannanase, endo-beta-(1->4)-mannanase, endo-beta-1,4 mannanase, endo-beta-1,4,D-mannanase, endo-beta-1,4-D-mannanase, endo-beta-1,4-mannanase, endo-beta-1,4-mannase, endo-beta-D-1,4-mannanase, endo-beta-D-mannanase, endo-beta-mannanase, endo-mannanase, GH 134 beta-1,4-mannanase, GH134, GH5-CBM27, KMAN-3, LeMAN4, LeMAN4a, Man, MAN I, Man II, MAN-P, Man1, Man113A, Man134A, Man26A, Man26A-50K, Man26b, Man4A, Man5, Man5A, Man5C, man5D, Man5P1, Man5XZ3, Man5_8, Man7, ManA, ManA/HmA, ManB, ManB-1601, ManC, ManEM17, ManF, ManH, ManIII, mannan endo-1,4-beta-mannanase, mannan endo-1,4-beta-mannosidase, mannan endo-1.4-beta-D-mannosidase, mannanase, mannanase, endo-1,4-beta-, ManP, ManS2, MYCTH_99077, PoMan5A, Rman, TpMan, TrMan5A

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.78 mannan endo-1,4-beta-mannosidase

General Stability

General Stability on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
although deleting carbohydrate binding module 10 increases the catalytic efficiency, its disruption decreases the pH, solvent and detergent stability of the enzyme
-
enzyme immobilization using cross-linked aggregated form (MB-C) and chitosan magnetic nanocomposites of MB-C leads to 73.2% higher activity (pH 4.0-9.0), up to 95.6% higher stability (pH 3.0-10.0, 9 h incubation at room temperature), up to 15°C higher optimal temperature, higher stability (up to 83%) in the presence of solvents and up to 1.62fold higher deactivation energy, as compared to the free enzyme. Immobilized enzymes are able to repeatedly hydrolyze locust bean gum till 12 cycles
enzyme is rather unstable and steadily loses activity during the purification process. Addition of 0.2% bovine serum albumine stabilizes
enzyme is resistant to digestion by trypsin
enzyme is strongly resistant to pepsin and trypsin digestion
the activity of enzyme immobilized onto chitosan coated magnetic nanoparticles is lost 21.4% after 10 cycles of reuse
-
the fused signal sequence of metalloprotease PrtA does not affect the enzymatic properties of the enzyme
-