Process Biochemistry, Vol.51, No.12, 2084-2089, 2016
Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant thermostable alkylsulfatase (SdsAP) from Pseudomonas sp S9
SdsAP, an efficient SOS degradation alkylsulfatase from Pseudomonas sp. S9, was immobilized in the form of cross-linked enzyme aggregates (CLEAs). Preliminary results revealed that over 80% activity of SdsAP-CLEAs was recovered using PEG4000 as the precipitating agent. Conditions for enzyme precipitation and cross-linking were further optimized. Compared to free SdsAP, SdsAP-CLEAs showed higher pH and temperature stability, and better tolerance to a certain organic solvents. Kinetic characterization analysis showed that SdsAP-CLEAs had higher affinity and catalytic efficiency than its soluble counterpart. Furthermore, SdsAP-CLEAs retained more-than 60% of their initial activity after 10 batches of re-use at 50 degrees C and little or no loss of activity after one month at 4 degrees C. These results suggested that immobilization with CLEAs could improve the stability and operability of SdsAP, exhibiting a great potential application of SdsAP-CLEAs on SDS degradation in industry wastewater treatment. (C) 2016 Elsevier Ltd. All rights reserved.