+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on Google+
Follow on LinkedIn
+ Translate
Investigation into the kinetic properties of immobilized lignin peroxidases
Presnell, T.L.; Swaisgood, H.E.; Joyce, T.W.; Chang, H.M.n, 1994: Investigation into the kinetic properties of immobilized lignin peroxidases. Journal of Biotechnology 35(1): 77-85
Mixtures of lignin peroxidase isozymes were immobilized onto controlled-pore glass (CPG) beads through three different functional groups (free amino groups, free carboxylate groups, or the aldehyde groups of the metaperiodate-oxidized carbohydrate portions of the proteins) and catalytic properties of the immobilized proteins were determined. Some loss of activity occurred in all immobilized samples, but relatively high activities were maintained with enzymes immobilized via the modified carbohydrate moieties. The effectiveness of using the immobilized enzymes to treat anthracene and pulp mill bleach plant effluent was tested. Bleach plant effluent precipitated onto the aminopropyl-CPG beads inactivating the enzymes, probably due to reactions with free amino groups. In contrast, anthracene was rapidly and completely degraded by the immobilized lignin peroxidases.Accession: 002416720
DOI: 10.1016/0168-1656(94)90191-0
Download PDF Full Text: Investigation into the kinetic properties of immobilized lignin peroxidases
Submit PDF Full Text
No spam - Every submission is manually reviewedDue to poor quality, we do not accept files from Researchgate
Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)
Select a PDF file:
Close
Related references