Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine

Akparov, V.K.; Konstantinova, G. E.; Тимофеев, В. И.; Khaliullin, Ilyas G.; Куранова, И. П.

doi:10.1016/j.bpc.2020.106535

Cited by 1 publication

(1 citation statement)

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“…Enzymes are very significant biocatalysts, which are widely used in food industry, [1] biocatalysis, [2] leather industry, [3] biosensor development, [4] biodiesel production [5] and other application fields owing to their high substrate selectivity, high catalytic efficiency, and mild reaction conditions [6–8] . However, there are some disadvantages in enzyme preparation, such as poor stability, [9] strict storage and transportation conditions, and poor recyclability, which greatly limits their practical applications.…”

Section: Introductionmentioning

confidence: 99%

Selective Immobilization of His‐Tagged Phosphomannose Isomerase on Ni Chelated Nanoparticles with Good Reusability and Activity

et al. 2022

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Self‐stable precipitation polymerization was used to prepare an enzyme‐immobilized microsphere composite. Phosphomannose isomerase (PMI) with His‐tag was successfully immobilized on Ni2+ charged pyridine‐derived particles. The maximum amount of PMI immobilized on such particles was ∼184 mg/g. Compared with free enzyme, the activity of the immobilized enzymes was significantly improved. In addition, the immobilized enzymes showed a much better thermostability than free enzymes. At the same time, the immobilized enzymes can be reused for multiple reaction cycles. We observed that the enzyme activity did not decrease significantly after six cycles. We conclude that the pyridine‐derived particles can be used to selectively immobilize His‐tagged enzymes, which can couple the enzyme purification and catalysis steps and improve the efficiency of enzyme‐catalyzed industrial processes.

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