Part F | 30
742 Part F Marine Derived Metabolites
worth noting them, although they are not related to the
carbohydrate chemistry but to protein and lipid fields.
A large number of Aplysia neuropeptides were identified and some of these biomolecules show remarkable
sequence similarities to mammalian neuropeptides. Enzymes acting specifically on these substrates could be
of interest for their specificity in the biocatalytic field
as well in other physiological studies [30.68, 69].
Lipoxygenases are also identified in Aplysia. These
enzymes act on lipids and are of interest for the
production of bioactive molecules both in vivo and
in vitro. Arachidonic acid is converted to (8R)-hydroperoxyeicosa-5,9,11,14-tetraenoic acid (8-HPETE)
during incubations with homogenates of the central
nervous system of the marine mollusc, Aplysia californica. The product can be then reduced to the
corresponding hydroxy acid or enzymatically converted to other metabolites [30.70]. In this field, enzymes of marine origin are characterized by regio
and stereoselective output of reactions different from
those found in terrestrial counterparts. From the synthetic chemist’s point of view asymmetric oxygenation reaction of unnatural substrates has a tremendous
potential [30.71].
30.6 Conclusion
Enzymatic routes are particularly useful to access new
products or for the modification of complex natural
products such as carbohydrates, which are very important molecules in various technological domains.
Herbivorous marine molluscs possessing various kind
of polysaccharide-degrading enzymes could efficiently
act on these molecules. These enzymes play important roles in the metabolism of the organism digesting
polymeric materials to oligosaccharides and monosaccharides as carbohydrate nutrients. They can also be
used in a diverse manner for biocatalyzed synthesis of
the glycosidic bond. Different interesting results related
to the presence of glycosyl hydrolases have been reported in the literature on Aplysia fasciata and Aplysia
kurodai. The examples have been judged to be of interest to the biocatalysis community. In A. fasciata ˇ-Dgalactosidase and ˛-D-glucosidase enzymes are present
in large amounts, and an interesting ˇ-mannosidase has
also been noticed; in A. kurodai different enzymes acting on polysaccharides were evidenced.
References
30.1
A. Trincone, A. Giordano: Glycosyl hydrolases
and glycosyl transferases in the synthesis of
oligosaccharides, Curr. Org. Chem. 10, 1163–1193
(2006)
30.2
P. Lorenz, J. Eck: Screening for novel industrial biocatalysts, Eng. Life Sci. 6, 501–504 (2004)
30.3
Q. Wang, J.S. Dordick, R.J. Linhardt: Synthesis and
application of carbohydrate-containing polymers,
Chem. Materials 14, 3232–3244 (2002)
30.4
S.I. Mussatto, I.M. Mancilha: Non-digestible oligosaccharides: A review, Carbohydr. Polymers 68,
587–597 (2007)
30.5
V. Kren: Glycoside vs. aglycon: The role of glycosidic residue in biological activity. In: Glycoscience
Chemistry and Chemical Biolog, ed. by B.O. FraserReid, K. Tatsuta and J. Thiem (Springer Berlin,
Heidelberg 2008) pp. 2589–2644
30.6
A. Trincone: Potential biocatalysts originating from
sea environments, J. Mol. Catal. B: Enzym. 66(3/4),
241–256 (2010)
30.7
A. Trincone: Some enzymes in marine environment: Prospective applications found in patent
literature, Recent Pat, Biotechnol. 6(2), 134–148
(2012)
30.8
A. Trincone: Marine biocatalysts: enzymatic features and applications, Mar. Drugs 9(4), 478–499
(2011)
30.9
A. Giordano, G. Andreotti, A. Tramice, A. Trincone:
Marine glycosyl hydrolases in the hydrolysis and
synthesis of oligosaccharides, Biotechnology J. 1(5),
511–530 (2006)
30.10 A. Tramice, G. Andreotti, A. Giordano, A. Trincone:
Enzymatic transglycosylation. In: Encyclopedia of
Industrial Biotechnology, Bioprocess, Bioseparation, and Cell Technology, ed. by M.C. Flickinger
(Wiley-VCH, Hoboken 2010) pp. 2071–2086
30.11 D.E. Koshland: Stereochemistry and the mechanism of enzymatic reactions, Biol. Rev. 28, 416–436
(1953)
30.12 V.L. Yip, S.G. Withers: Breakdown of oligosaccharides by the process of elimination, Curr. Opin.
Chem. Biol. 10, 147–155 (2006)
30.13 D. Vocadlo, G.J. Davies: Mechanistic insights into
glycosidase chemistry, Curr. Opin. Chem. Biol. 12,
539–555 (2008)
30.14 G. Davies, B. Henrissat: Structures and mechanisms of glycosyl hydrolases, Structure 3, 853–859
(1995)
742 Part F Marine Derived Metabolites
worth noting them, although they are not related to the
carbohydrate chemistry but to protein and lipid fields.
A large number of Aplysia neuropeptides were identified and some of these biomolecules show remarkable
sequence similarities to mammalian neuropeptides. Enzymes acting specifically on these substrates could be
of interest for their specificity in the biocatalytic field
as well in other physiological studies [30.68, 69].
Lipoxygenases are also identified in Aplysia. These
enzymes act on lipids and are of interest for the
production of bioactive molecules both in vivo and
in vitro. Arachidonic acid is converted to (8R)-hydroperoxyeicosa-5,9,11,14-tetraenoic acid (8-HPETE)
during incubations with homogenates of the central
nervous system of the marine mollusc, Aplysia californica. The product can be then reduced to the
corresponding hydroxy acid or enzymatically converted to other metabolites [30.70]. In this field, enzymes of marine origin are characterized by regio
and stereoselective output of reactions different from
those found in terrestrial counterparts. From the synthetic chemist’s point of view asymmetric oxygenation reaction of unnatural substrates has a tremendous
potential [30.71].
30.6 Conclusion
Enzymatic routes are particularly useful to access new
products or for the modification of complex natural
products such as carbohydrates, which are very important molecules in various technological domains.
Herbivorous marine molluscs possessing various kind
of polysaccharide-degrading enzymes could efficiently
act on these molecules. These enzymes play important roles in the metabolism of the organism digesting
polymeric materials to oligosaccharides and monosaccharides as carbohydrate nutrients. They can also be
used in a diverse manner for biocatalyzed synthesis of
the glycosidic bond. Different interesting results related
to the presence of glycosyl hydrolases have been reported in the literature on Aplysia fasciata and Aplysia
kurodai. The examples have been judged to be of interest to the biocatalysis community. In A. fasciata ˇ-Dgalactosidase and ˛-D-glucosidase enzymes are present
in large amounts, and an interesting ˇ-mannosidase has
also been noticed; in A. kurodai different enzymes acting on polysaccharides were evidenced.
References
30.1
A. Trincone, A. Giordano: Glycosyl hydrolases
and glycosyl transferases in the synthesis of
oligosaccharides, Curr. Org. Chem. 10, 1163–1193
(2006)
30.2
P. Lorenz, J. Eck: Screening for novel industrial biocatalysts, Eng. Life Sci. 6, 501–504 (2004)
30.3
Q. Wang, J.S. Dordick, R.J. Linhardt: Synthesis and
application of carbohydrate-containing polymers,
Chem. Materials 14, 3232–3244 (2002)
30.4
S.I. Mussatto, I.M. Mancilha: Non-digestible oligosaccharides: A review, Carbohydr. Polymers 68,
587–597 (2007)
30.5
V. Kren: Glycoside vs. aglycon: The role of glycosidic residue in biological activity. In: Glycoscience
Chemistry and Chemical Biolog, ed. by B.O. FraserReid, K. Tatsuta and J. Thiem (Springer Berlin,
Heidelberg 2008) pp. 2589–2644
30.6
A. Trincone: Potential biocatalysts originating from
sea environments, J. Mol. Catal. B: Enzym. 66(3/4),
241–256 (2010)
30.7
A. Trincone: Some enzymes in marine environment: Prospective applications found in patent
literature, Recent Pat, Biotechnol. 6(2), 134–148
(2012)
30.8
A. Trincone: Marine biocatalysts: enzymatic features and applications, Mar. Drugs 9(4), 478–499
(2011)
30.9
A. Giordano, G. Andreotti, A. Tramice, A. Trincone:
Marine glycosyl hydrolases in the hydrolysis and
synthesis of oligosaccharides, Biotechnology J. 1(5),
511–530 (2006)
30.10 A. Tramice, G. Andreotti, A. Giordano, A. Trincone:
Enzymatic transglycosylation. In: Encyclopedia of
Industrial Biotechnology, Bioprocess, Bioseparation, and Cell Technology, ed. by M.C. Flickinger
(Wiley-VCH, Hoboken 2010) pp. 2071–2086
30.11 D.E. Koshland: Stereochemistry and the mechanism of enzymatic reactions, Biol. Rev. 28, 416–436
(1953)
30.12 V.L. Yip, S.G. Withers: Breakdown of oligosaccharides by the process of elimination, Curr. Opin.
Chem. Biol. 10, 147–155 (2006)
30.13 D. Vocadlo, G.J. Davies: Mechanistic insights into
glycosidase chemistry, Curr. Opin. Chem. Biol. 12,
539–555 (2008)
30.14 G. Davies, B. Henrissat: Structures and mechanisms of glycosyl hydrolases, Structure 3, 853–859
(1995)