Add time:08/29/2019         Source:sciencedirect.com

Aminoacylases (EC 3.5.1.1.4) of Streptomyces ambofaciens ATCC 23877 were immobilized by chemical and physical adsorption onto SBA-15 mesoporous silica materials. The activity of the immobilized aminoacylases was firstly evaluated by considering the hydrolysis reactions of N-α-acetyl-lysine, used as rapid method of screening. After chemical adsorption, a significant loss of activity was observed probably due to a conformational change of the aminoacylases structures upon immobilization. When the immobilization was performed by physisorption a higher amount of enzyme (0.20 against 0.05 mg per mg of support) can be adsorbed onto the mesoporous silica material. The physisorbed biocatalyst also presented a higher hydrolytic activity than the chemisorbed enzyme. Recycling of the supported biocatalysts was performed three times with no loss of the specific activity. Furthermore, a better thermostability was also noted in comparison with free enzyme upon aminoacylases physisorption.Finally, lauroyl-lysine synthesis was catalyzed for the first time by immobilized aminoacylases. The crude extract from S. ambofaciens exhibited the rare ability to catalyze the N-acylation on amino group in the α-position of the lysine whereas the lipase B of Candida antarctica catalyzed the acylation of lysine on its amino group in ε-position. This particular and original regioselectivity was maintained with immobilized enzymes.

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