Enzyme systems in marine algae. The carbohydrase activities of unfractionated extracts of <i>Cladophora rupestris, Laminaria digitata, Rhodymenia palmata</i> and <i>Ulva lactuca</i>

Duncan, W. A. M.; Manners, D. J.; Ross, A. G.

doi:10.1042/bj0630044

Cited by 45 publications

(11 citation statements)

References 19 publications

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“…However, it does not differ between the control and each enzymatic treatment and may not influence the specific enzymatic action. Finally, the calculation of degradation percentage from the comparison between control and enzymatic digestion conditions may avoid having to account for non-specific hydrolysis by mechanical breaking and/or intrinsic proteolytic enzymes during the 6 h of agitation, as shown in some studies (Duncan et al 1956;Pérez-Lloréns et al 2003).…”

Section: Discussionmentioning

confidence: 99%

An evaluation of methods for quantifying the enzymatic degradation of red seaweed Grateloupia turuturu

et al. 2008

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For better exploitation of the red seaweed Grateloupia, enzymatic digestion of the thallus may be a way to increase access to metabolites of industrial interest. With this aim, we have tried to find a method to quantify the efficiency of enzymatic digestion. Vegetative algal material was treated with polysaccharidases (Onozuka R-10 cellulase, agarase, and Ultraflo L mixture). The proportion of degraded surface area was determined by microscopic measurement of the residue surface using imaging software and compared with the analysis of carbohydrates and Rphycoerythrin released in the incubation solution. Both the reducing carbohydrate concentration and percentage of degraded surface area appeared the most reliable methods to study enzymatic efficiency. The amount of solubilized total carbohydrates, and particularly that of R-phycoerythrin, showed non-specific variations, so no conclusions could be drawn. The application of this procedure to the screening of the efficient digestion of Grateloupia material demonstrated that cell walls were only partially digested by polysaccharidase enzymes alone. The Ultraflo L mixture and Onozuka R-10 cellulase produced a greater degradation of Grateloupia tissues and a higher release of reducing carbohydrates, whereas agarase did not display any specific action. Thus, the proposed procedure based on the quantification of residue surface area seems to be an accurate method to analyze enzymatic digestion. Other tests using different concentrations and combinations of enzymes are now required.

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Section: Discussionmentioning

confidence: 99%

An evaluation of methods for quantifying the enzymatic degradation of red seaweed Grateloupia turuturu

et al. 2008

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“…Enzymes catalyzing analogous transfer reactions have been reported in extracts of Bacillius inacerans (25), blood plasma (22), germinated green gram (24), and minced algae (6). Similarily, a recently reported cabbage leaf enzyme (17) produced several oligosaccharides from concentrated maltose solutions.…”

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confidence: 67%

Properties of Glucosyltransferase and Glucan Transferase from Spinach

Linden

Tanner²,

Kandler³

1974

Plant Physiol.

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A glucosyl and a glucosyl-glucan transferase activity from spinach (Spinacia oleracea L. var. Matador) leaves have been partially purified and characterized. The latter activity (fraction 1 after diethylaminoethylcellulose chromatography) is responsible for the transfer of glucosyl as well as of maltosyl, maltotriosyl, and higher homologous residues to glucose giving rise to maltose and the correspondingly larger molecules. This fraction also shows p-amylase activity. The transfer takes place only to glucose; maltose, as well as other ac-1,4-glucans, serve as donors. The enzyme fraction 2 is amylase-free and catalyzes only the transfer of glucosyl moieties, again with high acceptor specificity to glucose. Maltose and larger o-1,4-glucans, with the exception of maltotriose and maltotetraose, act as donors. The physiological function of these enzymes mav be the formation of oligosaccharide primers for starch synthetase or phosphorylase.Maltose was first recognized to participate in 1,4-to 1,4-glycosyl transfer reactions with extracellular enzymes of Escherichzia coli (1, 7), which synthesized members of the maltodextrin series from maltose. Enzymes catalyzing analogous transfer reactions have been reported in extracts of Bacillius inacerans (25), blood plasma (22), germinated green gram (24), and minced algae (6). Similarily, a recently reported cabbage leaf enzyme (17) produced several oligosaccharides from concentrated maltose solutions.In 1961 Edelman and Keys (8), described an enzyme from wheat germ which catalyzed the transfer of the nonreducing end glycosyl moiety of maltose to "C-glucose with reformation of "C-maltose, as in reaction 1.O-0 + 0* = 0-0*+In reactions 1 through 5, 0 represents a glucosyl unit, 0 represents a reducing glucosyl unit, 0* represents a "C-labeled glucosyl unit,-represents an a-1, 4-linkage, and represents continuation of such bonding as in amylose.The enzymatic activities described in this paper catalyzed reaction 1 as well as some reactions similar to, but not identical with, those of D-enzyme (EC 2.4.1 f; 1,4-glucan:a-1,4-glucan 4-glucosyltransferase) from potato (15,26,27,30,31). Other properties of the enzymatic reactions upon preliminary purification are described.MATERIALS AND METHODS Sources of Chemicals. Litner soluble starch and shellfish glycogen were purchased from Schuhardt, Munich. Amylopectin was prepared from fresh potato juice from which the amylose was precipitated with 1-butanol. Pure maltose was a generous gift from the laboratory of J. F. Robyt. Other maltodextrins were prepared from a fungal amylase digest of amylose precipitated three times (Sigma, St. Louis), separated on a charcoal-celite column (10), and purified by paper chromatography on formic acid and water-washed Whatman No. 1 paper. Other oligosaccharides were from commercial sources and were purified in the same way. Other materials were reagent grade.Radioactive compounds were obtained from the Radiochemical Centre. Amersham, with the exception of the following: 2-deoxy-glycose and a-D-glucos...

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“…MEEUSE and SMITH (1962) have shown that granular starches from Ulva sp., and Codium fragile are broken down by oc-amylase preparations from various sources, including that from the mollusc Cryptochiton stelleri; this finding is relevant to the grazing of marine animals on seaweeds. Extracts of various marine algae including Cladophora rupestris and Ulva lactuca show the presence of both oc-amylase and oc-glucosidase activity, which could degrade starch by a hydrolytic pathway to the monosaccharide level (DUNCAN et al 1956). However, the overall level of activity of these extracts was so low that enzyme fractionaction studies could not be carried out.…”

Section: The Metabolism Of Marine Algal Starchesmentioning

confidence: 99%

“…In the first, xylan containing both (1 -> 3) and (1 -> 4)-linkages is present either as a separate xylan, or combined in a heteropolysaccharide, neither of which is skeletal material. In the second, the xylan is a linear component of the cell wall, and is either completely (1 -> 4)-linked, or completely xylosides (DUNCAN et al 1956, MANNERS andMITCHELL 1967). These activities could presumably form a hydrolytic pathway for the catabolism of algal xylans.…”

Section: Xylansmentioning

confidence: 99%

Reserve Carbohydrates of Algae, Fungi, and Lichens

Manners¹,

Sturgeon²

1982

Plant Carbohydrates I

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Enzyme systems in marine algae. The carbohydrase activities of unfractionated extracts of Cladophora rupestris, Laminaria digitata, Rhodymenia palmata and Ulva lactuca

Abstract: Present knowledge of the metabolism-of terrestrial plants and freshwater algae is considerable (cf.

Cited by 45 publications

References 19 publications

An evaluation of methods for quantifying the enzymatic degradation of red seaweed Grateloupia turuturu

An evaluation of methods for quantifying the enzymatic degradation of red seaweed Grateloupia turuturu

Properties of Glucosyltransferase and Glucan Transferase from Spinach

Reserve Carbohydrates of Algae, Fungi, and Lichens

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