FIG 7.

Temperature stability of enzymes immobilized to GFP particles. The particles were preincubated at 4°C, 15°C, 25°C, 35°C, 45°C, 55°C, 65°C, 75°C, 85°C, and 95°C for 10 min and then subjected to their respective reactions. Activity is relative to the PhaC bead at 25°C. (A) Twenty-five micrograms of NanA-PhaC or GiCLN fusion protein reacted with 0.2 M N-acetyl-d-mannosamine and 1 M sodium pyruvate at 50°C. The production of N-acetyl neuraminic acid was quantified by HPLC. (B) Fifty micrograms of Bla(−ss)-PhaC or GiCLB fusion protein reacted with 1% starch solution at 25°C. The release of maltose was quantified by the α-amylase colorimetric assay. (C) Fifty micrograms of PhaC-OpdA or GiCLO fusion protein reacted with 200 μM methyl parathion at 25°C. The release of paranitrophenol was quantified by spectroscopy. Error bars are ±1 standard deviation (n = 3). G, GFP; iC, inactive PhaC; L, linker; N, NanA; B, BLA; O, OpdA.