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Colloidal gold labelling of l,4‐β‐D‐glucan cellobiohydrolase adsorbed on cellulose substrates
Author(s) -
Chanzy H.,
Henrissat B.,
Vuong R.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81124-2
Subject(s) - trichoderma reesei , adsorption , chemistry , colloidal gold , cellulose , crystal (programming language) , glucan , crystallography , colloid , materials science , biochemistry , cellulase , nanoparticle , nanotechnology , organic chemistry , computer science , programming language
The 1,4‐β‐D‐glucan cellobiohydrolase I (CBHI) from Trichoderma reesei was labelled with 4–6 nm gold particles. This CBHI‐gold complex still retains 60% of the original CBHI activity and allows good visualization of the enzyme adsorbed at the surface of cellulose mirofibrils or microcrystals. The main features of the adsorption are: rapid and irreversible binding; preference of the crystal edges instead of the crystal surface for the binding; the absence of specificity for the crystal tips where the cellulose chain ends are supposedly located.