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Figure S1. Lineweaver–Burke plots of PBS wash buffer removed from 30% PEGDA crosslinked gels where 1/[s] (1/M) is the concentration of ONPG substrate and 1/v (min*liter/mol) is 1/(the velocity of enzymatic conversion). a: 1st wash fluid at 3 h containing initial, non-entrapped enzyme, and unreacted reagents. b: 20 min later, 2nd wash fluid containing leached enzyme from the drop cast biogel. The apparent lack of linear regression fit proves no active enzyme leached into solution. c: 30% PEGDA crosslinked gels after 2nd wash proving maintained enzyme entrapment and no leaching at approximately 3 h post-entrapment.

Figure S2. Lineweaver–Burke plot of enzyme entrapped within 2% (w/v) alginate gels showing no linear regession fit and therefore no retention of activity. Where 1/[s] (1/M) is the concentration of ONPG substrate and 1/v (min*liter/mol) is 1/(the velocity of enzymatic conversion).

Figure S3. Sample graphs showing calculation methods for Vmax and Km. a: Conversion of ONPG substrate into ONP product at 3 h post-entrapment of various initial concentrations of substrate ONPG in 5% BIS crosslinked gel. b: Lineweaver–Burke plot of 5% BIS crosslinked gels at 3 h post-entrapment, where 1/[s] in 1/M is the concentration of substrate, and 1/v in min*liter/mol is 1/(the velocity of enzymatic conversion, seen as the slope in Supplementary Figure 3a).

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