THE ENZYMIC HYDROLYSIS OF CARRAGEENAN BY PSEUDOMONAS CARRAGEENOVORA: PURIFICATION OF A κ-CARRAGEENASE

1966 ◽  
Vol 12 (5) ◽  
pp. 939-947 ◽  
Author(s):  
J. Weigl ◽  
W. Yaphe
Keyword(s):  
Degradation Product ◽  
Culture Medium ◽  
Deae Cellulose ◽  
Reducing Power ◽  
Enzymic Hydrolysis ◽  
Specific Viscosity ◽  
Sulfated Oligosaccharides ◽  
Rapid Fall ◽  
Hydrolysis Of ◽  
Major Degradation Product

Enzymes specific for the κ and λ fractions of carrageenan were obtained from the cell-free culture medium of Pseudomonas carrageenovora. These enzymes were concentrated by precipitation with ammonium sulfate and separated by chromatography on hydroxylapatite.The κ-carrageenase was purified to electrophoretic homogeneity by incubation at 35 °C and chromatography on DEAE cellulose. The enzymic hydrolysis of κ-carrageenan was accompanied by a rapid fall in specific viscosity and increase in reducing power. The products were a homologous series of sulfated oligosaccharides with 3-O-(3,6-anhydro-α-D-galactopyranosyl)-D-galactopyranose-4-O-sulfate (neocarrabiose-4-O-sulfate) as the major degradation product, and an enzyme-resistant fraction. The alkali-modified enzyme-resistant fraction was degraded by the κ-carrageenase.

Enzymic hydrolysis of the potassium chloride soluble fraction of carrageenan: properties of "λ-carrageenases" from Pseudomonas carrageenovora

1973 ◽  
Vol 19 (7) ◽  
pp. 779-788 ◽  
Author(s):  
K. H. Johnston ◽  
E. L. McCandless
Keyword(s):  
Soluble Fraction ◽  
Reducing Sugar ◽  
Chondrus Crispus ◽  
Enzymic Hydrolysis ◽  
Temperature Optimum ◽  
Ph Optimum ◽  
Specific Viscosity ◽  
Chromatographic Resolution ◽  
Fraction I ◽  
Hydrolysis Of

An enzyme complex which hydrolyzed the KCl soluble carrageenan extracted from the red alga Chondrus crispus has been isolated from the cell-free medium of a culture of Pseudomonas carrageenovora grown on this polysaccharide. Three hydrolases could be separated. Fraction I, which caused a rapid decrease in the specific viscosity of the polysaccharide preparation with only minimal release of reducing sugar, could be distinguished from fraction II chromatographically on Sephadex G-100 and electrophoretically on agarose gel. Fraction IIa caused release of reducing sugar at pH 6.2, which activity was depressed at pH 7.5. Fraction IIb exhibited viscometric activity only at both pH 6.2 and pH 7.5. Fraction IIa had a sharp pH optimum at pH 6.2 and a temperature optimum at 28°. All hydrolases were inactivated by freezing, by dialysis against distilled water, by heating at 35° for 30 min, and by Hg2+ and 0.0001 mM EDTA. When fraction II (a and b) isolated after chromatographic resolution on Sephadex G-100 was incubated at pH 6.2 with KCl soluble carrageenan from C. crispus, products which had Rgal values of 0.74 and 0.17 were detected, were sulfated, and contained no 3,6-anhydrogalactose.

scholarly journals CHARACTERIZATION OF ENZYMES HYDROLYZING ACYL NAPHTHYLAMIDES: II. TRIHALOGEN DERIVATIVES

1965 ◽  
Vol 13 (2) ◽  
pp. 117-124 ◽  
Author(s):  
V. K. HOPSU ◽  
R. S. SANTTI ◽  
G. G. GLENNER
Keyword(s):  
Species Differences ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Enzymic Hydrolysis ◽  
Hydrolysis Rates ◽  
Starch Gel ◽  
Acylase I ◽  
Hydrolysis Of ◽  
Substrate Hydrolysis

Enzymes in guinea pig homogenates hydrolyzing a variety of halogenated and nonhalogenated acyl α- and β-naphthylamide substrates can be separated into two major groups on the basis of substrate hydrolysis rates, solubility and affector characteristics. Both groups of enzymes, those acting on the non-, mono- and dihalogenated acyl naphthylamides and those acting on trihalogen derivatives, have characteristics like those of arylesterases and are inseparable from enzymes hydrolyzing naphthol AS acetate. These enzymes are, However, separable on fractionation by starch gel electrophoresis and DEAE-cellulose chromatography from several enzymes catalyzing the hydrolysis of N-acyl amino acids (acylase I and II) and several amino acid β-naphthylamides. Species differences exist in the characteristics of enzymic hydrolysis of these acylarylamides.

Variation in Quantity of Methanol Recovered from Raisins

1963 ◽  
Vol 46 (2) ◽  
pp. 341-343
Author(s):  
M Alice Brown ◽  
James R Woodward ◽  
Floyd DeEds
Keyword(s):  
Methyl Ester ◽  
Esterase Activity ◽  
Enzymic Hydrolysis ◽  
Methanol Content ◽  
Naturally Occurring ◽  
Pectin Esterase ◽  
Hydrolysis Of

Abstract The amount of naturally occurring methanol in fruit must be known so that the quantity left as fumigation residue can be determined. In a study of methanol content of raisins, which had given inconsistent results, the raisins were subjected to different conditions of treatment immediately prior to methanol determination. Conditions that favored pectin esterase activity gave higher values for methanol content than conditions known to inactivate enzymes. Evidence was also obtained that both chemical and enzymic hydrolysis of methyl ester groups of pectic materials occur during analysis.

scholarly journals Permeability of muscle capillaries to small heme-peptides. Evidence for the existence of patent transendothelial channels.

1975 ◽  
Vol 64 (3) ◽  
pp. 586-607 ◽  
Author(s):  
N Simionescu ◽  
M Siminoescu ◽  
G E Palade
Keyword(s):  
Plasma Proteins ◽  
Intercellular Junctions ◽  
Rat Diaphragm ◽  
Enzymic Hydrolysis ◽  
Graphic Analysis ◽  
Heme Peptides ◽  
Future Work ◽  
Hydrolysis Of ◽  
Muscle Capillaries

Two heme-peptides (HP) of about 20-A diameter (heme-undecapeptide [H11P], mol wt approximately 1900 and heme-octapeptide [H8P], mol wt approximately 1550), obtained by enzymic hydrolysis of cytochrome c, were sued as probe molecules in muscle capillaries (rat diaphragm). They were localized in situ by a perixidase reaction, enhanced by the addition of imidazole to the incubation medium. Chromatography of plasma samples showed that HPs circulate predominantly as monomers for the duration of the experiments and are bound by aldehyde fixatives to plasma proteins to the extent of approximately 50% (H8P) to approximately 95% (H11P). Both tracers cross the endothelium primarily via plasmalemmal vesicles which become progressively labeled (by reaction product) from the blood front to the tissue front of the endothelium, in three successive resolvable phases. By the end of each phase the extent of labeling reaches greater than 90% of the corresponding vesicle population. Labeled vesicles appear as either isolated units or chains which form patent channels across the endothelium. The patency of these channels was checked by specimen tilting and graphic analysis of their images. No evidence was found for early or preferential marking of the intercellular junctions and spaces by reaction product. It is concluded that the channels are the most likely candidate for structural equivalents of the small pores of the capillary wall since they are continuous, water-filled passages, and are provided with one or more strictures of less than 100 A. Their frequency remains to be established by future work.

Investigation of the products of an enzymic hydrolysis of collagens

Biochemistry ◽  
1969 ◽  
Vol 8 (12) ◽  
pp. 4716-4723 ◽  
Author(s):  
Howard B. Bensusan
Keyword(s):  
Enzymic Hydrolysis ◽  
Hydrolysis Of

scholarly journals Constancy of the optimum temperature of an enzyme under varying concentrations of substrate and of enzyme

1914 ◽  
Vol 88 (602) ◽  
pp. 258-262
Keyword(s):  
Experimental Evidence ◽  
Aspergillus Oryzae ◽  
Hydrolytic Enzyme ◽  
Fixed Duration ◽  
Optimum Temperature ◽  
Enzymic Hydrolysis ◽  
Main Interest ◽  
General Law ◽  
The Moment ◽  
Hydrolysis Of

In a recent paper a new enzymic relation is recorded. For the enzymic hydrolysis of salicin—by the enzyme which Gabriel Bertrand and the author have named salicinase —it is found that, in an action of fixed duration, the temperature of greatest activity of the ferment is always the same, whatever the dilutions of substrate and of enzyme adopted for the determination. In other words, the duration of the action being constant, the optimum tem­perature of the ferment is independent of the concentration both of the substrate and of the enzyme. The observation is suggestive: if true of one enzyme it may be true of all, and possibly becomes the enunciation of a general law. Herein, for the moment, lies its main interest. In the present paper further experimental evidence for this hypothesis in given, in the case of another hydrolytic enzyme, the maltase of Aspergillus oryzæ (taka-diastase).

Covalent attachment of amino acids to casein. 1. Chemical modification and rates of in vitro enzymic hydrolysis of derivatives

1979 ◽  
Vol 27 (5) ◽  
pp. 1098-1104 ◽  
Author(s):  
Antoine J. Puigserver ◽  
Lourminia C. Sen ◽  
Elvira Gonzales-Flores ◽  
Robert E. Feeney ◽  
John R. Whitaker
Keyword(s):  
Amino Acids ◽  
Chemical Modification ◽  
Covalent Attachment ◽  
Enzymic Hydrolysis ◽  
Hydrolysis Of
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