Enzymes have great potential in industrial applications, but utilizing them at high efficiency levels, especially above room temperature, has not been fully realized. The immobilization of papain onto homo-functionalized silica gel via multipoint covalent attachment has successfully addressed this issue, resulting in a stable and reusable enzyme catalyst with improved activity and adaptability to higher temperatures.
Although enzymes play a significant role in industrial applications, their potential usage at high-level efficiency, particularly above room temperature, has not yet been fully harnessed. It brings above room-temperature catalytic sustainability of an immobilized (imm.) bio-catalyst as a long pending issue to improve enzyme stability, activity, specificity, or selectivity, particularly the enantio-selectivity over the native-enzymes. At this juncture, in a robust methodology, a heterogeneous solid phase bio-catalyst, {Si(OSi)4(H2O)1.03}n= 3 2 8{OSi(CH3)2-NH-C6H4-N= N}4{papain}(H2O)251, has efficiently been prepared by immobilizing papain on homo-functionalized SG (silica-gel) via multipoint covalent attachment. The bio-catalyst is easy to be recovered and reused multiple times. The homo-functional -N=N+, which appears on the SG-surface, makes the multipoint diazo-links with the inert center of the tyrosine-moiety to couple the enzyme where all the amino, thiol, phenol, and so forth, groups of the protein, including those that belong to the active-site, remain intact. The immobilized enzyme (13.9 smol g-1) swims in pore-water within the pore-channel, remains stable up to 70 +/- 5 degrees C, and exhibits wider temperature adaptability in performing its hydrolyzing activities. The relative activity, 78 +/- 2% at 27 degrees C, remains quantitative for 60 days and can be reused for 60 cycles with 53% activity at room-temperature. The thermal (relative activity: 87%; incubated at 70 +/- 5 degrees C for 24 h) and mechanical (relative activity: 92%; incubated at 2500 rpm for 2 h at 27 degrees C) stability was outstanding.
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