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https://www.selleckchem.com/products/i-138.html A zein-degrading protease (ZDP) from Zea mays was heterologously expressed using Pichia pastoris and its characteristics and effects on enzymatic hydrolysis of corn starch were investigated in the current study. The optimal temperature and pH for ZDP activity was 40 °C and pH 5.0, respectively. The ZDP exhibited a degree of thermal stability and was repressed by some metal ions (5 mM) including Zn2+, Mg2+, Cu2+, Mn2+, Ni2+, K+, and Ca2+, especially Mn2+ and Cu2+, which caused near complete inhibition. Dithiothreitol and β-mercaptoethanol (5 mM) could tremendously increase the ZDP activity by 102.1% and 60.7%, respectively. The ZDP could not tolerate organic solvents such as ethanol, acetone, and dimethyl sulphoxide. The ZDP could efficiently degrade the pure commercial zein and the native zein in the corn, increase the leaching of corn soluble sugars, destroy the cross-linked starch-zein structure, and release the starch granules, consequently increasing the α-amylase hydrolysis of corn starch. The recombinant ZDP might be useful to improve the utilization of corn.A biogenic mesoporous silica nanoparticles (MSNs)-based nanocarrier has been used for improving the stability and recyclability of PersiXyn2 as a recombinant xylanase enzyme. The biogenic MSNs (called RKIT-6 henceforth) were synthesized via a soft templating method using rice husk biomass as a renewable silica source. Then bis-(2-aminoethyl) ether modified RKIT-6 (denoted as bis-AE@RKIT-6) was prepared through the furnishing surface with bis-(2-aminoethyl) ether, as a pendant anchoring agent to immobilize PersiXyn2. The nanomaterials were characterized using nitrogen adsorption-desorption isotherms, atomic force microscopy (AFM), X-ray diffraction (XRD), molecular docking (MD) study, and thermogravimetric analysis (TGA). After immobilizing, PersiXyn2@bis-AE@RKIT-6, the optimal temperature of enzyme performance was improved more than 10 °C in comparison with t

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