Degradation of algal (Ascophyllum nodosum) fucoidan by an enzymatic activity contained in digestive glands of the marine mollusc Pecten maximus

Daniel, Régis; Berteau, Olivier; Jozefonvicz, J.; Goasdoué, N.

doi:10.1016/s0008-6215(99)00223-2

Cited by 79 publications

(32 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The NMR data obtained here for A. nodosum fucoidan showed that two types of glycosidic bonds linked L-fucose units in this polysaccharide, i.e. a-(1!4) and a-(1!3), as we and others had previously proposed from studies of more complex and heavier fucoidan fractions [4,7]. It is worthwhile noting that different fucoidans from other brown algae species such as Fucus vesiculosus [8], Ecklonia kurome [25], Chorda filum [26], and Cladosiphon okamuranus [27] have been described in the literature that all involve only the a-(1 !3) linkage.…”

Section: O N C L U S I O N Ssupporting

confidence: 79%

Regioselective desulfation of sulfated l-fucopyranoside by a new sulfoesterase from the marine mollusk Pecten maximus. . Application to the structural study of algal fucoidan (Ascophyllum nodosum)

Daniel¹,

Berteau²,

Chevolot³

et al. 2001

Eur J Biochem

Self Cite

View full text Add to dashboard Cite

The study of the structural bases of the biological properties of algal fucoidan (Ascophyllum nodosum ) led us to look for enzymes able to modify this sulfated polysaccharide. In this context, we found a sulfoesterase activity in the digestive glands of the common marine mollusk Pecten maximus, which is active on fucoidan. This sulfoesterase activity was shown by capillary electrophoresis and 13 C-1 H NMR (500 MHz) analysis of the enzymatic hydrolysis of the fucoidan, of fucoidan oligosaccharides and of sulfated fucose isomers. We report the exhaustive list of all proton and carbon chemical shifts for each of the three isomers of sulfated-L-fucose (including of their a/b anomers), i.e. the 2-O-, 3-O-and 4-O-sulfated fucose, which have been useful reference values for the assignments of NMR spectra of fucoidan oligosaccharides upon enzymatic desulfation. Our results demonstrated a high regioselectivity for this sulfoesterase, which hydrolyzes only the sulfate group at the 2-O position of the fucopyranoside. Therefore, this sulfoesterase is a helpful tool in the structure -activity study of the fucoidan, as the literature data suggest that the 2-Osulfation level play a central role in the biological properties of the polysaccharide.

show abstract

Section: O N C L U S I O N Ssupporting

confidence: 79%

Regioselective desulfation of sulfated l-fucopyranoside by a new sulfoesterase from the marine mollusk Pecten maximus. . Application to the structural study of algal fucoidan (Ascophyllum nodosum)

Daniel¹,

Berteau²,

Chevolot³

et al. 2001

Eur J Biochem

Self Cite

View full text Add to dashboard Cite

show abstract

“…Fucoidanase can be found in marine bacteria such as Pseudomonas atlantica, Pseudomonas carrageenovora, Pseudomonas alteromonas, Vibrio sp., Bacillus sp. HTP2, Pseudoalteromonas citrea, (Sakai et al 2002;Urvantseva et al 2006); marine invertebrates such as Haliotis sp., sea cucumber (Sakai et al 2003a,b,c,d), sponges and molluscs (Daniel et al 1999), and marine fungi D. arenaria TM94 (Wu et al 2002), Fusarium sp. LD8 , Aspergillus niger, Penicillium purpurogenum, Mucor sp.…”

Section: Discussionmentioning

confidence: 99%

Purification and characteristics of fucoidanase obtained from Dendryphiella arenaria TM94

Zhang

et al. 2010

J Appl Phycol

View full text Add to dashboard Cite

Dendryphiella arenaria TM94 is an obligate marine fungus. Fucoidanase expressed by TM94 by solid state fermentation was purified. The fermented solid medium was extracted with citric acid buffer, and the extracts were precipitated by acetone and separated on Sephadex G-100 chromatography. The specific fucoidanase activity of purified enzyme was 27-fold than that of the crude enzyme. The recovery of the enzyme was 17.69%. SDS-PAGE was used to identify the purity and the molecular weight of the fucoidanase. A single band appeared on SDS-PAGE gel which suggested that relatively pure fucoidanase has been obtained. The molecular weight of fucoidanase is 180 kDa and the isoelectric point was about pH 4.4. The purified fucoidanase appeared to have the maximum enzymatic activity at pH 6.0. K M and the maximum velocity of the enzyme was 6.56 mg·mL −1 and 6.55 mg·mL −1 ·min −1 by using fucoidan from Fucus vesiculosus as substrate. The enzyme may be a type of endo-fucoidanase which could hydrolyze high molecular weight fucoidan to low molecular weight fucoidan rather than to fucose.

show abstract

“…Until now, enzymes that degrade fucoidans were found in the following marine organisms: bacteria [25,26,27], invertebrates [28,29,30,31,32] and some fungi [33]. However, the fucoidanases produced by these organisms have low activities.…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae

et al. 2013

View full text Add to dashboard Cite

Intracellular fucoidanase was isolated from the marine bacterium, Formosa algae strain KMM 3553. The first appearance of fucoidan enzymatic hydrolysis products in a cell-free extract was detected after 4 h of bacterial growth, and maximal fucoidanase activity was observed after 12 h of growth. The fucoidanase displayed maximal activity in a wide range of pH values, from 6.5 to 9.1. The presence of Mg2+, Ca2+ and Ba2+ cations strongly activated the enzyme; however, Cu2+ and Zn2+ cations had inhibitory effects on the enzymatic activity. The enzymatic activity of fucoidanase was considerably reduced after prolonged (about 60 min) incubation of the enzyme solution at 45 °C. The fucoidanase catalyzed the hydrolysis of fucoidans from Fucus evanescens and Fucus vesiculosus, but not from Saccharina cichorioides. The fucoidanase also did not hydrolyze carrageenan. Desulfated fucoidan from F. evanescens was hydrolysed very weakly in contrast to deacetylated fucoidan, which was hydrolysed more actively compared to the native fucoidan from F. evanescens. Analysis of the structure of the enzymatic products showed that the marine bacteria, F. algae, synthesized an α-l-fucanase with an endo-type action that is specific for 1→4-bonds in a polysaccharide molecule built up of alternating three- and four-linked α-l-fucopyranose residues sulfated mainly at position 2.

show abstract

Degradation of algal (Ascophyllum nodosum) fucoidan by an enzymatic activity contained in digestive glands of the marine mollusc Pecten maximus

Cited by 79 publications

References 22 publications

Regioselective desulfation of sulfated l-fucopyranoside by a new sulfoesterase from the marine mollusk Pecten maximus. . Application to the structural study of algal fucoidan (Ascophyllum nodosum)

Regioselective desulfation of sulfated l-fucopyranoside by a new sulfoesterase from the marine mollusk Pecten maximus. . Application to the structural study of algal fucoidan (Ascophyllum nodosum)

Purification and characteristics of fucoidanase obtained from Dendryphiella arenaria TM94

Hydrolysis of Fucoidan by Fucoidanase Isolated from the Marine Bacterium, Formosa algae

Contact Info

Product

Resources

About