By R.J. Sturgeon

In recent times the main major advances in carbohydrate study were made within the wisdom of the constitution and serve as of carbohydrates within the macromolecular nation. This name addresses these parts of the topic within which the authors think an important paintings is being conducted.

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Extra resources for Advances in Macromolecular Carbohydrate Research, Volume 1

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Awamori AXH [88] have been recently isolated from Pseudomonas fluorescens [167], wheat [145], Bifidobacterium adolescentis [168], and T, reesei (R. Kavitha, unpublished work). Two further similar enzymes have been isolated from B. polymyxa, although in addition to hydrolyzing arabinoxylans, these enzymes also have very low, but detectable activity against aryl-a-L-arabinofuranosides, but no other arabinose containing substrates [169]. Physicochemical properties of some of these enzymes are given in Table 16.

For the degradation and tailored modification of arabinans, the active and most efficient enzymes have to be identified and their action patterns studied at a molecular level. This will boost the production of these enzymes and improve their properties by DNA technology. Arabinans and Arabinan Degrading Enzymes 41 V. APPENDIX: REVIEW OF THE LITERATURE 1992-1997 The preceding sections of this review were prepared and accepted for publication in 1992. Since there has been considerable research into arabinans and arabinan degrading enzymes in the last few years, at our request, the editor allowed us to review the recently published findings which are summarized below.

Niger S. 0; 30 °C; /7-nitrophenyl-a-L-arabinofuranoside. 5; 30 °C; p-nitrophenyl-a-L-arabinofuranoside. be used, referring to this type of enzyme as arabinofuranosidase B (Arafur B). Properties of the enzyme has been reviewed by Kaji [32] and Whitaker [31]. Its appearance in nature is extensive, including fungi, bacteria, actinomycetes, yeasts, protozoa, and plants. However, in order to compare the different arabinofuranosidases B properly, discussion will be restricted to those enzymes which have been purified and characterized in more detail.

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