By R.J. Sturgeon
In recent times the main major advances in carbohydrate examine were made within the wisdom of the constitution and serve as of carbohydrates within the macromolecular country. This name addresses these parts of the topic within which the authors think crucial paintings is being performed.
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Extra info for Advances in Macromolecular Carbohydrate Research, Volume 1
Purpurascens. Earlier investigations on A. niger arabinanases failed to identify arabinofuranosidase A, probably because a heat treatment was introduced to facilitate the isolation of another type of arabinofuranosidase [91,92]. This latter enzyme was shown to be more heat-stable then arabinofuranosidase A . Enzyme stability studies indicated the existence of two types of arabinofuranosidase in^. niger [31,93]. One form appeared to be stable at pH 4 and the other one at pH 7. However, in the original paper it was stated that this was caused by two forms of the same enzyme, being another type than arabinofuranosidase A.
137 A2+A3 149 138, 149 172,173 50 BELDMANETAL. with the A. niger enzyme having five binding subsites and the A. aculeatus enzyme six . The extent and rate of branched arabinan hydrolysis by all ewrfo-arabinanases appears affected by the degree of substitution on the arabinan backbone by (l->3)- or (l->2)-a-L-arabinofuranosyl residues [19,30,117,137,173]. ^^C-NMR studies of hydrolysis products released from branched arabinan by the A. , 3^-a-L-arabinofuranosyl (l-»5)-a-L-arabinotriose]. This suggested a requirement for this enzyme of at least one unsubstituted a-L-arabinofuranosyl residue on either side of the substituted residue before hydrolysis can occur.
0. An optimum pH for bacterial arabinofuranosidases appears to be more in the neutral region. C. rolfsii and R. flava produce an enzyme which is active at extreme acidic conditions. K^ values of all purified arabinofuranosidases are of the same order of magnitude. -nitrophenyl- aL-arabinofuranoside. The two—^probably different—strains of ^. niger produce arabinofuranosidases with different properties, especially with respect to molecular weights and isoelectric points (Table 6). The best characterized enzyme has been isolated from^.
Advances in Macromolecular Carbohydrate Research, Volume 1 by R.J. Sturgeon