β-1,3-1,4-Glucanase

β-1,3-1,4-Glucanase (30 min) shows optimal activity at pH 6.0 and 55 °C, and is activated by Mg²⁺/Na⁺ but inhibited by Hg²⁺/Ag⁺^[1].
β-1,3-1,4-Glucanase (1% (w/v) substrate; 55 °C) exhibits high specific activity towards barley β-glucan (425 U/mg), oat β-glucan (392 U/mg), and lichenin (212 U/mg), with low activity towards laminarin and no activity towards other tested substrates^[1].
β-1,3-1,4-glucanase (1.0% lichenan; 10 min at 60°C) expressed in transgenic maize seeds (generations T₁, BC₁, BC₂, BC₃) exhibits stable, high-level activity, with BC₃ seeds reaching a maximal activity of 779,800 U/kg^[2].
β-1,3-1,4-Glucanase and its H58D/D235G mutants can boost the hydrolysis of pretreated corn stover, with both mutants yielding more reducing sugars than the wild-type enzyme^[3].
β-1,3-1,4-glucanase (FsGlc16A) (200 U/g oat bran; 8 h) hydrolyzes endogenous enzyme-deactivated oat bran into trisaccharide and tetrasaccharid after 8 h incubation at 50 ◦C and pH 4.5^[4].

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