Stability and carbohydrate composition of chloroperoxidase from Caldariomyces fumago grown in a fructose–salts medium

1988 ◽  
Vol 34 (8) ◽  
pp. 998-1002 ◽  
Author(s):  
Michael A. Pickard ◽  
Atsumi Hashimoto
Keyword(s):  
Gas Chromatography ◽  
Enzyme Activity ◽  
Acid Hydrolysis ◽  
Composition Studies ◽  
Malt Extract ◽  
Carbohydrate Composition ◽  
Isoelectric Focussing ◽  
Caldariomyces Fumago ◽  
Carbohydrate Components

The glycoprotein chloroperoxidase has been isolated from Caldariomyces fumago grown in a fructose-salts medium and some of its properties studied, including stability to pH and temperature and carbohydrate composition, as a preliminary to immobilization. At 22 °C, more than 50% of the activity remained after 15 days when the enzyme was maintained between pH 3.5 and 5.5; between pH 6 and 7 only 25% of activity remained after 4 days. At 40 °C and pH 5.5, enzyme activity was stable for 7 days. Carbohydrate composition studies were carried out on six isoenzymes of chloroperoxidase that were separated by isoelectric focussing on flat-bed Sephadex G-75 gels. After acid hydrolysis and derivatization, the carbohydrate components of the isoenzymes were analyzed by gas chromatography. The major components were found to be glucose and mannose, with xylose, galactose, and glucosamine present at levels less than 10% of the total. These results contrasted with those for the enzyme purified after growth of the fungus on glucose and malt extract, previously reported, where the carbohydrate components were identified as arabinose and glucosamine.

A defined growth medium for the production of chloroperoxidase by Caldariomyces fumago

1981 ◽  
Vol 27 (12) ◽  
pp. 1298-1305 ◽  
Author(s):  
Michael A. Pickard
Keyword(s):  
Enzyme Activity ◽  
Carbon Source ◽  
Growth Medium ◽  
Enzyme Production ◽  
Defined Medium ◽  
Malt Extract ◽  
Caldariomyces Fumago ◽  
High Enzyme ◽  
Extract Medium ◽  
Malt Extract Medium

Ten strains of Caldariomyces fumago and related fungi were found to produce extracellular chloroperoxidase when grown on a glucose – malt extract medium. High enzyme levels and pigment production were observed for C. fumago ATCC 16373 and C. fumago CMI 89362. Removal of malt extract from the medium and the replacement of glucose by fructose as the carbon source provided a defined medium which, by comparison with the complex medium, produced the following results with both fungal strains. Chloroperoxidase was produced to similar levels, with maximum production after 6 days rather than 12 days of growth; pigmentation of the medium was reduced by 90% and the pH of the medium remained constant, thus stabilizing enzyme activity. Addition of urea or proline as a nitrogen supplement to nitrate enhanced enzyme production by strain CMI 89362. Comparison of the two strains indicated that CMI 89362 produced higher levels of chloroperoxidase than ATCC 16373.

scholarly journals PEMBUATAN BIOETANOL DARI KUPASAN KENTANG (Solanum tuberosum L.) DENGAN PROSES FERMENTASI

Jurnal Kimia ◽  
2016 ◽  
Author(s):  
Devi Esteria Hasianna Purba ◽  
Iryanti Eka Suprihatin ◽  
A.A.I.A. Mayun Laksmiwati
Keyword(s):  
Gas Chromatography ◽  
Renewable Energy ◽  
Solanum Tuberosum ◽  
Acid Hydrolysis ◽  
Sulphuric Acid ◽  
Solanum Tuberosum L ◽  
Alternative Source ◽  
Hydrolysis Process ◽  
Potato Peels ◽  
Detoxification Process

Ethanol fermented from potato peels is proposed as one alternative source of renewable energy called bioethanol. In this research bioethanol was produced through four stages namely acid hydrolysis, detoxification, fermentation and distillation. The acid hydrolysis process was carried out using sulphuric acid at 100oC for 60 minutes. The detoxification process was carried out by adding NH4OH into the hydrolyzate prior to fermentation. Distillation was performed up to 100oC and the distillate with the BP of 78-84oC was determined for its ethanol content using gas chromatography. The ethanol produced from 5 grams of dried potato peels through fermentation for 4, 5, 6, and 7 days 3.54%; 4,85%; 5,35%; and 6.15% respectively.

scholarly journals Identification of phosphorylated 3-deoxy-manno-octulosonic acid as a component of Haemophilus influenzae lipopolysaccharide

1987 ◽  
Vol 245 (2) ◽  
pp. 583-587 ◽  
Author(s):  
S E Zamze ◽  
M A J Ferguson ◽  
E R Moxon ◽  
R A Dwek ◽  
T W Rademacher
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Alkaline Phosphatase ◽  
Haemophilus Influenzae ◽  
Acid Hydrolysis ◽  
Reliable Method ◽  
Gas Chromatography Mass Spectrometry ◽  
Chromatography Mass Spectrometry ◽  
Rough Mutant

A phosphorylated 3-deoxy-manno-octulosonic acid (KDO) was released from the lipopolysaccharide (LPS) of the deep rough mutant (Rb+169) of Haemophilus influenzae by acid hydrolysis. Both phosphorylated and dephosphorylated KDO, produced by treatment with alkaline phosphatase, were identified by gas chromatography-mass spectrometry after trimethylsilylation. This technique provides a rapid and reliable method for the identification of phosphorylated KDO in LPS.

Further studies on the differentiation of Clostridium sordellii from Clostridium bifermentans by gas chromatography

1970 ◽  
Vol 16 (11) ◽  
pp. 1071-1078 ◽  
Author(s):  
John B. Brooks ◽  
V. R. Dowell ◽  
D. C. Farshy ◽  
A. Y. Armfield
Keyword(s):  
Gas Chromatography ◽  
The Other ◽  
Gas Liquid Chromatography ◽  
Carbohydrate Composition ◽  
Whole Cells ◽  
Cultural Medium ◽  
Urease Production ◽  
Clostridium Bifermentans ◽  
Trimethylsilyl Derivatives ◽  
Derivatives Of

Amines produced by 31 strains of the Clostridium bifermentans and C. sordellii groups were compared by examining trifluoroaceticanhydride derivatives of basic chloroform extracts from spent cultural medium by gas–liquid chromatography (g.l.c.). All of the urease-positive strains (16) exhibited an amine profile consistent with that of C. sordellii. On the other hand, 12 of 15 urease-negative strains produced amine g.l.c. patterns like that of C. bifermentans, and three strains produced amine patterns identical with that of C. sordellii. The carbohydrate composition of some of the strains was determined by g.l.c. of trimethylsilyl derivatives of acid-digested formamide extracts of whole cells. Two of the three urease-negative strains with amine profiles like C. sordellii had a carbohydrate composition similar to that of C. sordellii, and the other strain had a carbohydrate profile more like that of C. bifermentans. One known strain of C. bifermentans had a carbohydrate profile with characteristics of both C. bifermentans and C. sordellii. The results of this study point out the variability of urease production by C. sordellii and the value of gas chromatography in differentiating this organism from C. bifermentans.

scholarly journals Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

1983 ◽  
Vol 215 (3) ◽  
pp. 483-489 ◽  
Author(s):  
F Serafini-Cessi ◽  
F Dall'Olio
Keyword(s):  
Sialic Acid ◽  
Guinea Pig ◽  
Acid Hydrolysis ◽  
Transferase Activity ◽  
Carbohydrate Composition ◽  
Mild Acid Hydrolysis ◽  
Enzymic Digestion ◽  
Pig Kidney ◽  
Mild Acid

A beta-N-acetylgalactosaminyltransferase that preferentially transferred N-acetylgalactosamine to Sd(a-) Tamm-Horsfall glycoprotein was found in guinea-pig kidney microsomal preparations. This enzyme was kidney-specific and was able to transfer the sugar to other glycoproteins, such as fetuin and alpha 1-acidic glycoprotein. The presence of sialic acid in the acceptors was essential for the transferase activity when either glycoproteins or their Pronase glycopeptides were used as acceptors. Two glycopeptides (Tamm-Horsfall glycopeptides I and II) with a different carbohydrate composition were separated by DEAE-Sephacel chromatography from Pronase-digested Tamm-Horsfall glycoprotein. The amount of N-acetylgalactosamine transferred to glycopeptides by the enzyme correlated with their degree of sialylation. Enzymic digestion of N-[14C]acetylgalactosamine-labelled Tamm-Horsfall glycopeptide II showed that the transferred sugar was susceptible to beta-N-hexosaminidase. The amount of sugar cleaved by beta-hexosaminidase was strongly increased when the labelled Tamm-Horsfall glycopeptide II was pretreated with mild acid hydrolysis, a procedure that removed the sialic acid residues. Alkaline borohydride treatment of the labelled Tamm-Horsfall glycopeptide II did not release radioactivity, thus indicating that enzymic glycosylation took place at the N-asparagine-linked oligosaccharide units of Tamm-Horsfall glycoprotein.

scholarly journals The influence of sialic acid residues on the ability of glycoproteins toi nteract electrostatically with chondromucoprotein

1965 ◽  
Vol 97 (2) ◽  
pp. 333-339 ◽  
Author(s):  
AJ Anderson
Keyword(s):  
Sialic Acid ◽  
Complex Formation ◽  
Acid Hydrolysis ◽  
Acid Content ◽  
Biological Activities ◽  
Carbohydrate Composition ◽  
Mild Acid Hydrolysis ◽  
Sialic Acid Content ◽  
Neuraminidase Treatment ◽  
Mild Acid

1. Although glycoproteins with less than 1% of sialic acid (fibrinogen, lipoproteins, gamma-globulins) interact electrostatically with chondromucoprotein to form insoluble complexes, interaction with glycoproteins containing larger amounts of sialic acid (orosomucoid, urine glycoprotein, seromucoid, fraction VI) was electrostatically impossible. Reasons for this are discussed. 2. The latter glycoproteins interacted with chondromucoprotein after mild acid hydrolysis or neuraminidase treatment, complex-formation being inversely related to their sialic acid content. 3. Complex-formation with sialic acid-deficient orosomucoid was maximum at pH3.6 and negligible above its isoelectric point of pH5, and was inhibited by Ca(2+) ions and EDTA. 4. These results are discussed in relation to the carbohydrate composition and biological activities of euglobulin fractions, and of complexes formed by adding chondromucoprotein to abnormal plasmas which may contain sialic acid-deficient glycoproteins owing to faulty carbohydrate metabolism.

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