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Literature summary for 3.8.1.5 extracted from

  • Zheng, H.; Yu, W.L.; Guo, X.; Zhao, Y.Z.; Cui, Y.; Hu, T.; Zhong, J.Y.
    An effective immobilized haloalkane dehalogenase DhaA from Rhodococcus rhodochrous by adsorption, crosslink and PEGylation on meso-cellular foam (2019), Int. J. Biol. Macromol., 125, 1016-1023 .
    View publication on PubMed

General Stability

General Stability Organism
immobilized enzyme exhibits a high stability in the extreme environmental conditions. The enzyme (DhaA) suffers from poor environmental stability and difficult recovery, which significantly increase the cost of DhaA. An effective enzyme immobilization strategy is developed to overcome the disadvantages of DhaA. DhaA is physically absorbed with amine-functionalized meso-cellular foam. The MCF-absorbed enzyme is intermolecularly crosslinked with 8-arm PEG N-hydroxysuccinimide ester and then PEGylated by maleimide-thiol chemistry Rhodococcus rhodochrous

Organic Solvent Stability

Organic Solvent Comment Organism
dimethyl sulfoxide immobilized enzyme shows 99.8% remaining activity in 40% (v/v) dimethylsulfoxide for 5 h Rhodococcus rhodochrous
urea immobilized enzyme shows 87.3% remaining activity in 3 M urea solution for 1 h Rhodococcus rhodochrous

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous P0A3G2
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Synonyms

Synonyms Comment Organism
DhaA
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Rhodococcus rhodochrous

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
23
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immobilized enzyme shows 51.8% at room temperature for 30 days Rhodococcus rhodochrous

pH Stability

pH Stability pH Stability Maximum Comment Organism
3
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immobilized enzyme shows 25.9% remaining activity at pH 3.0 Rhodococcus rhodochrous