Preparation and characterization of cross-linked enzyme aggregates (CLEAs) of recombinant thermostable alkylsulfatase (SdsAP) from Pseudomonas sp. S9

[Display omitted] •SdsAP, an alkylsulfatase for SDS degradation, was immobilized as CLEAs with high activity.•SdsAP-CLEAs showed higher pH and temperature stability, and better tolerance to a certain organic solvents.•SdsAP-CLEAs had higher affinity and catalytic efficiency than its soluble counterpart.•SdsAP-CLEAs also showed good reusability and storage resistance.•The stability and operability of SdsAP-CLEAs exhibiting a great potential application of on SDS degradation in industry wastewater treatment. SdsAP, an efficient SDS 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°C and little or no loss of activity after one month at 4°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.