Elsevier

Carbohydrate Research

Volume 71, Issue 1, June 1979, Pages 205-230
Carbohydrate Research

Enzymic hydrolysis, fine structure, and gelling interaction of legume-seed d-galacto-d-mannans

https://doi.org/10.1016/S0008-6215(00)86071-1Get rights and content

Abstract

The fine structure of d-galacto-d-mannans was analyzed with purified α-d-galactosidases from germinated lucerne seed and from green coffee beans and with a commercial β-d-mannanase (Driselase). Each of the α-d-galactosidase enzymes removed d-galactosyl residues from the d-mannan backbone in a random fashion; α-d-galactosidase A from lucerne removed more than 90% of the d-galactosyl groups from each of the ten native d-galacto-d-mannans studied. Mixtures of purified α-d-galactosidase C and β-d-mannanase B from lucerne hydrolyzed each of the ten d-galacto-d-mannans to d-galactose, β-d-mannobiose, and β-d-mannotriose, with trace amounts of d-mannose. The degrees of hydrolysis by β-d-mannanase of native d-galacto-d-mannans, and of lucerne d-galacto-d-mannan pre-hydrolyzed by α-d-galactosidase, are dependent on the galactose contents. The amounts of oligosaccharides produced from native d-galacto-d-mannans by Driselase β-d-mannanase parallel those obtained from lucerne d-galacto-d-mannan that had been pre-hydrolyzed to similar galactose levels with α-d-galactosidase, except for the d-galacto-d-mannans of Leucaena leucocephala and soybean, which are hydrolyzed with β-d-mannanase to a higher degree. A direct correlation between the extent of hydrolysis of d-galacto-d-mannans by β-d-mannanase and the degree of gelling interaction with xanthan gum was observed, suggesting that interaction of d-galacto-d-mannans with xanthan does not absolutely require long sections of contiguous unsubstituted d-mannose residues but rather sections where all the galactosyl residues are located on one side of the main chain and may also serve as “junction zones”.

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