10.1111/j.1432-1033.1983.tb07808.x
Crossref journal-article
Wiley
European Journal of Biochemistry (311)
Abstract

β‐Agarase I and II were characterised by their action on agar‐type polysaccharides and oligosaccharides.β‐Agarase I, an endo‐enzyme, was specific for regions containing a minimum of one unsubstituted neoagarobiose unit [3,6‐anhydro‐α‐l‐galactopyranosyl‐(1 → 3)‐d‐galactose], hydrolysing at the reducing side of this moiety. Yaphe demonstrated that agar was degraded by this enzyme to neoagaro‐oligosaccharides limited by the disaccharide but with a predominance of the tetramer [Yaphe, W. (1957) Can. J. Microbiol. 3, 987–993]. β‐Agarase I slowly degraded neoagarohexaose but not the homologous tetrasaccharide. [1‐3H] Neoagarohexaitol was cleaved to neoagarotetraose and [1‐3H]neoagarobiitol. The highly substituted agar, porphyran was degraded to methylated, sulphated and unsubstituted neoagaro‐oligosaccharides which were invariably terminated at the reducing end by unsubstituted neoagarobiose.The novel enzyme, β‐agarase II, was shown to be an endo‐enzyme. Preliminary evidence indicated this enzyme was specific for sequences containing neoagarobiose and/or 61‐O‐methyl‐neoagarobiose. It degraded agar to neoagaro‐oligosaccharides of which the disaccharide was limiting and predominant. β‐Agarase II rapidly degraded isolated neoagarotetraose and neoagarohexaose to the disaccharide. With [1‐3H]neoagarohexaitol, exo‐action was observed, the alditol being cleaved to neoagarobiose and [1‐3H]neoagarotetraitol. Neoagarotetraitol was hydrolysed at 4% of the rate observed for the hexaitol. Porphyran was degraded to oligosaccharides, the neutral fraction comprising 24% of the starting carbohydrate. This fraction was almost exclusively disaccharides (22.4%) containing neoagarobiose (7.4%) and 61‐O‐methyl‐neoagarobiose (15%). β‐Agarase II is probably the ‘β‐neoagarotetraose hydrolase’ reported by Groleau and Yaphe as an exoenzyme against neoagaro‐oligosaccharides [Groleau, D. and Yaphe, W. (1977) Can. J. Microbiol. 23, 672–679].

Bibliography

MORRICE, L. M., McLEAN, M. W., LONG, W. F., & WILLIAMSON, F. B. (1983). β‐Agarases I and II from Pseudomonas atlantica. European Journal of Biochemistry, 137(1–2), 149–154. Portico.

Authors 4
  1. Lora M. MORRICE (first)
  2. Maitland W. McLEAN (additional)
  3. William F. LONG (additional)
  4. Frank B. WILLIAMSON (additional)
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Dates
Type When
Created 20 years, 5 months ago (March 3, 2005, 5:48 p.m.)
Deposited 2 years ago (Aug. 31, 2023, 5:04 a.m.)
Indexed 3 weeks ago (Aug. 12, 2025, 5:24 p.m.)
Issued 41 years, 9 months ago (Dec. 1, 1983)
Published 41 years, 9 months ago (Dec. 1, 1983)
Published Online 20 years, 5 months ago (March 3, 2005)
Published Print 41 years, 9 months ago (Dec. 1, 1983)
Funders 0

None

@article{MORRICE_1983, title={β‐Agarases I and II from Pseudomonas atlantica: Substrate specificities}, volume={137}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1983.tb07808.x}, DOI={10.1111/j.1432-1033.1983.tb07808.x}, number={1–2}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={MORRICE, Lora M. and McLEAN, Maitland W. and LONG, William F. and WILLIAMSON, Frank B.}, year={1983}, month=dec, pages={149–154} }