journal article Open Access May 27, 2015

Seaweed Hydrocolloid Production: An Update on Enzyme Assisted Extraction and Modification Technologies

Marine Drugs Vol. 13 No. 6 pp. 3340-3359 · MDPI AG
View at Publisher Save 10.3390/md13063340
Abstract
Agar, alginate, and carrageenans are high-value seaweed hydrocolloids, which are used as gelation and thickening agents in different food, pharmaceutical, and biotechnological applications. The annual global production of these hydrocolloids has recently reached 100,000 tons with a gross market value just above US$ 1.1 billion. The techno-functional properties of the seaweed polysaccharides depend strictly on their unique structural make-up, notably degree and position of sulfation and presence of anhydro-bridges. Classical extraction techniques include hot alkali treatments, but recent research has shown promising results with enzymes. Current methods mainly involve use of commercially available enzyme mixtures developed for terrestrial plant material processing. Application of seaweed polysaccharide targeted enzymes allows for selective extraction at mild conditions as well as tailor-made modifications of the hydrocolloids to obtain specific functionalities. This review provides an update of the detailed structural features of κ-, ι-, λ-carrageenans, agars, and alginate, and a thorough discussion of enzyme assisted extraction and processing techniques for these hydrocolloids.
Topics

No keywords indexed for this article. Browse by subject →

References
73
[1]
The Sea Weed Site: Information on Marine Algae. Available online: http://seaweed.ie/uses_general/industrialgums.php.
[2]
Mchugh, D.J. (2003). A Guide to the Seaweed Industry, Food and Agriculture Organization of the United Nations. FAO Fisheries Technical Paper 441.
[3]
Msuya "The impact of seaweed farming on the socioeconomic status of coastal communities in Zanzibar, Tanzania" World Aquac. (2011)
[4]
McHugh, D. (1987). Production and Utilization of Products from Commercial Seaweeds, Food and Agriculture Organization of the United Nations. FAO Fisheries Technical Paper 288.
[5]
Peppelman "On the structure of κ/ι-hybrid carrageenans" Carbohydr. Res. (2001) 10.1016/s0008-6215(01)00054-4
[6]
Valderrama, D., Cai, J., Hishamunda, N., and Ridler, N. (2013). Social and Economic Dimensions of Carrageenan Seaweed Farming, Food and Agriculture Organization of the United Nations. Fisheries and Aquaculture Technical Paper 580.
[7]
Rudolph "Carrageenan biotechnology" Trends Food Sci. Technol. (1997) 10.1016/s0924-2244(97)01091-1
[8]
Poinas "The cyclization of the 3,6-anhydro-galactose ring of iota-carrageenan is catalyzed by two d-galactose-2,6-sulfurylases in the red alga Chondrus crispus" Plant Physiol. (2009) 10.1104/pp.109.144329
[9]
Wang "Successful preparation and characterization of biotechnological grade agarose from indigenous Gelidium amansii of Taiwan" Process. Biochem. (2012) 10.1016/j.procbio.2011.12.015
[10]
Biological interactions between polysaccharides and divalent cations: The egg‐box model

Gregor T. Grant, Edwin R. Morris, David A. Rees et al.

FEBS Letters 1973 10.1016/0014-5793(73)80770-7
[11]
Torres "Extraction and physicochemical characterization of Sargassum vulgare alginate from Brazil" Carbohydr. Res. (2007) 10.1016/j.carres.2007.05.022
[12]
Usov "Polysaccharides of the red algae" Adv. Carbohydr. Chem. Biochem. (2011) 10.1016/b978-0-12-385520-6.00004-2
[13]
Knutsen "A modified system of nomenclature for red algal galactans" Bot. Mar. (1994) 10.1515/botm.1994.37.2.163
[14]
Rochas "Sulfate content of carrageenan and agar determined by infrared spectroscopy" Bot. Mar. (1986) 10.1515/botm.1986.29.4.335
[15]
Knutsen "1H and 13C high resolution NMR spectroscopy of carrageenans: Application in research and industry" Trends Food Sci. Technol. (2002) 10.1016/s0924-2244(02)00066-3
[16]
Cole, K., and Sheath, R. (1990). Biology of the Red Algae, Cambridge University Press.
[17]
Montero "Effects of Na+, K+ and Ca2+ on gels formed from fresh mince containing a carrageenan or alginate" Food Hydrocoll. (2002) 10.1016/s0268-005x(01)00110-2
[18]
Gulrez, S.K.H., Al-Assaf, S., and Phillips, G.O. (2011). Progress in Molecular and Environmental Bioengineering—From Analysis and Modeling to Technology Applications, InTech. Chapter 5.
[19]
Rees "Structure, conformation and mechanism in the formation of polysaccharide gels and networks" Adv. Carbohydr. Chem. Biochem. (1969) 10.1016/s0065-2318(08)60352-2
[20]
Wu, P., and Imai, M. (2012). Novel Biopolymer Composite Membrane Involved with Selective Mass Transfer and Excellent Water Permeability, InTech. 10.5772/50697
[21]
Bono "Effect of process conditions on the gel viscosity and gel strength of semi-refined carrageenan (SRC) produced from seaweed (Kappaphycus alvarezii)" J. King Saud Univ. Eng. Sci. (2012) 10.1016/j.jksues.2012.06.001
[24]
Montero "Enzyme-assisted extraction of κ/ι-hybrid carrageenan from Mastocarpus stellatus for obtaining bioactive ingredients and their application for edible active film development" Food Funct. (2014) 10.1039/c3fo60310e
[25]
Rodrigues "Iota-carrageenans from Solieria filiformis (Rhodophyta) and their effects in the inflammation and coagulation" Acta Sci. Technol. (2012)
[26]
Varadarajan, S.A., Ramli, N., Ariff, A., Said, M., and Yasir, S.M. (2009, January 9–11). Development of high yielding carragenan extraction method from Eucheuma Cotonii using cellulase and Aspergillus niger. Proceedings of Prosiding Seminar Kimia Bersama UKM-ITB VIII, Bangi, Malaysia.
[27]
Fleurence "Use of enzymatic cell wall degradation for improvement of protein extraction from Chondrus crispus, Gracilaria verrucosa and Palmaria palmata" J. Appl. Phycol. (1995) 10.1007/bf00003796
[28]
Kulshreshtha "Enzyme-assisted extraction of bioactive material from Chondrus crispus and Codium fragile and its effect on Herpes simplex virus (HSV-1)" Mar. Drugs (2015) 10.3390/md13010558
[29]
Potin "Processing and hydrolytic mechanism of the cgkA-encoded κ-carrageenase of Alteromonas carrageenovora" Eur. J. Biochem. (1995) 10.1111/j.1432-1033.1995.tb20348.x
[30]
Barbeyron "Iota-carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases" J. Biol. Chem. (2000) 10.1074/jbc.m003404200
[31]
Guibet "Degradation of λ-carrageenan by Pseudoalteromonas carrageenovora λ-carrageenase: A new family of glycoside hydrolases unrelated to κ- and ι-carrageenases" Biochem. J. (2007) 10.1042//bj20061359
[32]
Lemoine "Physical state of kappa-carrageenan modulates the mode of action of kappa-carrageenase from Pseudoalteromonas carrageenovora" Biochem. J. (2009) 10.1042/bj20080619
[33]
Michel "The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: A novel insight in the evolution of Clan-B glycoside hydrolases" Structure (2001) 10.1016/s0969-2126(01)00612-8
[34]
Henares "Iota-carrageenan hydrolysis by Pseudoalteromonas carrageenovora IFO12985" Philipp. J. Sci. (2010)
[35]
Ma "Purification, cloning, characterization and essential amino acid residues analysis of a new ι-carrageenase from Cellulophaga sp. QY3" PLoS ONE (2013) 10.1371/journal.pone.0064666
[36]
McLean "Neocarratetraose 4-O-monosulphate P-hydrolase from Pseudomonas carrageenovora" Eur. J. Biochem. (1981) 10.1111/j.1432-1033.1981.tb05084.x
[37]
McLean "Glycosulphatase from Pseudomonas carrageenovora" Eur. J. Biochem. (1979) 10.1111/j.1432-1033.1979.tb19744.x
[38]
Genicot "Controlling carrageenan structure using a novel formylglycine-dependent sulfatase, an endo-4S-iota-carrageenan sulfatase" Mar. Biotechnol. (2013) 10.1007/s10126-012-9483-y
[39]
Raman "The heparin/heparan sulfate 2-O-sulfatase from Flavobacterium heparinum: A structural and biochemical study of the enzyme active site and saccharide substrate specificity" J. Biol. Chem. (2003) 10.1074/jbc.m211425200
[40]
Renn "Biotechnology and the red seaweed polysaccharide industry: Status, needs and prospects" Trends Biotechnol. (1997) 10.1016/s0167-7799(96)10069-x
[41]
Li "Carrageenan and its applications in drug delivery" Carbohydr. Polym. (2014) 10.1016/j.carbpol.2013.12.008
[42]
Wong "Sulfohydrolase activity and carrageenan biosynthesis in Chondrus crispus (Rhodophyceae)" Plant Physiol. (1978) 10.1104/pp.61.4.663
[43]
Rees "Enzymic desulphation of porphyran" Biochem. J. (1961) 10.1042/bj0800449
[44]
Ohta "Purification and Characterization of a novel a-agarase from a Thalassomonas sp." Curr. Microbiol. (2005) 10.1007/s00284-004-4435-z
[45]
Wang "Characterization of a novel β-agarase from marine Alteromonas sp. SY37-12 and its degrading products" Appl. Microbiol. Biotechnol. (2006) 10.1007/s00253-005-0207-3
[46]
Haraguchi "Purification and propertes of poly(β-d-mannuronate) lyase from Azotobacter chroococcum" Appl. Microbiol. Biotechnol. (1996) 10.1007/bf00172488
[47]
Boyd "Isolation of poly-alpha-l-guluronate lyase from Klebsiella aerogenes" Carbohydr. Res. (1977) 10.1016/s0008-6215(00)81928-x
[48]
Haug "Biosynthesis of Alginate: Part II. Polymannuronic acid C-5-epimerase from Azotobacter vinelandii" Carbohydr. Res. (1971) 10.1016/s0008-6215(00)82537-9
[49]
Rees "Enzymic synthesis of 3:6-anhydro-l-galactose within porphyran from l-galactose 6-sulphate units" Biochem. J. (1961) 10.1042/bj0810347
[50]
Araki "Studies on the chemical constitution of agar-agar" Bull. Chem. Soc. Jpn. (1967) 10.1246/bcsj.40.1452

Showing 50 of 73 references