ArticleBioprocess and biosystems engineering2022
Preparation, characterization and stability of cross linked nitrilase aggregates (nitrilase-CLEAs) for hydroxylation of 2-chloroisonicotinonitrile to 2-chloroisonicotinic acid.
Article in Bioprocess and biosystems engineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 10 citations in OpenAlex.
- Enzymatic approaches to nicotinic acid synthesis: recent advances and future prospects.Frontiers in bioengineering and biotechnology · 2025Review
- Nitrilase GiNIT fromInternational journal of molecular sciences · 2024Article
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3 authors at 1 institution in 1 country.
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Abstract
Nitrilases capable of performing hydroxylation of 2-chloroisonicotinonitrile to 2-chloroisonicotinic acid were screened, and ES-NIT-102 was the best nitrilase for said biotransformation. Nitrilase was immobilized as cross linked enzyme aggregates (nitrilase-CLEAs) by fractional precipitation with iso-propanol, and cross linked with glutaraldehyde. The nitrilase-CLEAs prepared with optimized 35 mM glutaraldehyde for 120 min cross linking time had 82.36 ± 4.45% residual activity, and displayed type-II structural CLEAs formation as confirmed by particle size, SEM, FTIR, and SDS-PAGE analysis. Nitrilase-CLEAs had superior pH and temperature stability, showed a shift in optimal temperature by 5 °C, and retained nearly 1.5 to 1.7 folds activity over free nitrilase at 50 °C and 55 °C after more than 9 h incubation. Nitrilase-CLEAs showed reduced affinity and decreased conversion of substrate as indicated by slightly higher K
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