Endo-1,4-β-mannanase

Endo-1,4-β-mannanase (1 mM; 1-16 h) remains stable for 1 h at 60 °C and for 16 h within a pH range of 5.0-9.0, and it is strongly inhibited by 1 mM Hg^2+[1].

Endo-1,4-β-mannanase (ManP) is isolated from Paenibacillus sp. strain HY-8. Its purified form, ManP, exhibits the highest biocatalytic activity toward locust bean gum, with a specific activity of 695 U mg^-1[2].
Endo-1,4-β-mannanase exhibits the highest biocatalytic activity toward locust bean gum at pH 7; its activity increases gradually from pH 3.5 to 7, and decreases when pH is higher than 7^[2].
Endo-1,4-β-mannanase exhibits the highest biocatalytic activity toward locust bean gum at 55°C; its activity increases from 30°C to 55°C and decreases rapidly at temperatures above 55°C^[2].
Endo-1,4-β-mannanase (1-5 mM; 10 min)​ exhibits enhanced biocatalytic activity toward locust bean gum in the presence of Mn²⁺, Co²⁺, Ca²⁺, Ba²⁺, Triton X-100, sodium azide and N-ethylmaleimide; is completely inhibited by Hg²⁺ and N-bromosuccinimide; and is partially inhibited by EDTA and Cu^2+[2].
Endo-1,4-β-mannanase (5 μg; 12 h) hydrolyses locust bean gum, ivory nut mannan and manno-oligosaccharides M₂-M₅ into smaller manno-oligosaccharides and a small amount of mannose, with distinct product profiles for each substrate, while the enzyme shows no activity towards non-mannoside polysaccharides^[2].
Endo-1,4-β-mannanase binds tightly to Avicel and ivory nut mannan, but does not bind to chitin, chitosan, curdlan, insoluble oat xylan, lignin, or poly (3-hydroxybutyrate) particles^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.