Immobilization of procerain B, a cysteine endopeptidase, on amberlite MB-150 beads.
Where this comes from
- Record sourced from PubMed, PMID 23776589.
- Also identified by DOI 10.1371/journal.pone.0066000 and PMC identifier 3679035.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Proteases are involved in several crucial biological processes and reported to have important physiological functions. They also have multifarious applications in different industries. The immobilized form of the enzyme further improves its industrial applicability. Here, we report covalent immobilization of a novel cysteine endopeptidase (procerain B) on amberlite MB-150 beads through glutaraldehyde by Schiff base linkage. The immobilized product was examined extensively by Fourier Transform Infrared Spectroscopy (FTIR), Scanning electron microscopy (SEM) and Energy Dispersive X-ray (EDX) analysis. The characterization of the immobilized product showed broader pH and thermal optima compared to the soluble form of the enzyme. The immobilized form of procerain B also showed lower Km (180.27±6 µM) compared to the soluble enzyme using azocasein as substrate. Further, immobilized procerain B retains 38.6% activity till the 10(th) use, which strongly represents its industrial candidature.
Medical subject headings
- Cysteine Endopeptidases
- Enzymes, Immobilized
- Resins, Synthetic