By R.J. Sturgeon
In recent times the main major advances in carbohydrate learn were made within the wisdom of the constitution and serve as of carbohydrates within the macromolecular kingdom. This identify addresses these components of the topic within which the authors think an important paintings is being conducted.
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Additional info for Advances in Macromolecular Carbohydrate Research, Volume 1
Acetobuylicum , while other Arafur B's from P. capsulatum  and B. fibrisolvens  were reported to show no activity against arabinogalactan, although branched arabinan and arabinoxylans were hydrolyzed rapidly. Two other arabinofuranosidases with more unusual substrate specificities were recently isolated from G. candidum . Like typical arafur A's, these enzymes hydrolyzed pnitrophenyl-a-L-arabinofuranoside but had no activity against branched beet arabinan. However, irrespective of this, they are probably best considered as arafur B's due to their ability to hydrolyze arabinogalactan and arabinoglucuronoxylan.
Enzymes with both P-D-xylopyranosidase and a-L-arabinofuranosidase activity have also been reported. Again, the purity of such enzymes has been questioned, although in contrast to Arabinans and Arabinan Degrading Enzymes 51 the "arabinose-releasing e«(io-xylanases", firm evidence to support the existence of these enzymes has been reported in the form of multifunctional cloned enzymes [180-182]. The properties of some of these enzymes with high arabinofuranosidase activity are shown in Table 18.
While all arafur B's, by definition, have activity against aryla-L-arabinofuranosides and a-L-arabinose containing oligo- and polysaccharides, some of the recently isolated enzymes appear to show some diversity in their substrate specificities. For example, most arafur B's hydrolyze branched arabinan and also have at least some activity against linear arabinan, arabinoxylan, and arabinogalactan, although the relative rate of hydrolysis of these substrates varies markedly between different enzymes.