化学
降级(电信)
降水
酶
色谱法
假单胞菌
热稳定性
催化作用
核化学
生物化学
有机化学
细菌
生物
遗传学
电信
物理
气象学
计算机科学
作者
Shengping Li,Yintao Su,Yadan Liu,Lifang Sun,Minxiang Yu,Yunkun Wu
标识
DOI:10.1016/j.procbio.2016.09.013
摘要
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.
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