Intracellular activity of mycelial proteinases during fruit-body development in Flammulina velutipes

1987 ◽  
Vol 65 (3) ◽  
pp. 518-525 ◽  
Author(s):  
Ema E. Chao ◽  
Hans E. Gruen
Keyword(s):  
Specific Activity ◽  
Proteinase Inhibitors ◽  
Fruit Body ◽  
Water Soluble ◽  
Flammulina Velutipes ◽  
Unit Weight ◽  
Protein Activity ◽  
Body Development ◽  
Water Soluble Protein ◽  
Rapid Elongation

In the mycelium of Flammulina velutipes cultured on potato–glucose solution the concentration of water-soluble protein began to decrease steeply before fruit bodies formed, but the total amount of protein per culture decreased only when fruit bodies began to elongate rapidly. The level remained very low during rapid elongation. Proteinase activity per unit weight of mycelium against milk protein and azoalbumin decreased in parallel with the concentration of mycelial protein. Activity against azure blue – hide powder was low until the onset of rapid fruit-body elongation and reached a maximum later during that phase. Azoalbumin was hydrolyzed more actively than hide powder. Proteolytic activity per gram of mycelium against mycelial protein was almost the same before fruiting as during rapid fruit-body elongation. Specific activities per milligram protein against the three types of nonnative substrates increased in parallel to a maximum late during rapid elongation when protein concentration was lowest. Specific activity against native mycelial protein was also higher in extracts from older mycelia. Proteolysis was optimal near neutral pH and very low at pH 3.2. Tests with group-specific proteinase inhibitors showed that metallo-proteinases predominate in the mycelium. Serine, and to a lesser extent carboxyl and thiol proteinases, were also present. Neither endogenous inhibitors nor activators of proteolysis were detected.

Distribution of cellular amino acids, protein, and total organic nitrogen during fruit body development in Flammulina velutipes. II. Growth on potato–glucose solution

1982 ◽  
Vol 60 (8) ◽  
pp. 1342-1351 ◽  
Author(s):  
Hans E. Gruen ◽  
William M. Wong
Keyword(s):  
Amino Acids ◽  
Organic Nitrogen ◽  
Glucose Solution ◽  
Fruit Body ◽  
Amino Nitrogen ◽  
Dry Weight ◽  
Early Growth ◽  
Flammulina Velutipes ◽  
Total Organic Nitrogen ◽  
Rapid Elongation

In Flammulina velutipes grown on potato–glucose solution the dry weight of mycelium decreased when fruitbodies elongated rapidly. Loss of dry weight by aborted primordia and stunted fruitbodies paralleled gains by large fruitbodies. These gains exceeded the losses by the rest of the colony and indicate that large fruitbodies derived their substrates both from the medium and from materials stored in the rest of the colony. Close to 43% of the organic nitrogen in the medium was consumed before fruitbodies formed and only 8% remained at the end of their growth. Concentrations of total nitrogen, α-amino nitrogen, and alkali-soluble protein declined in the mycelium during most of the growth of the fruitbodies and then remained constant except for a slight final increase in protein. Concentrations of these fractions also decreased in the small fruitbodies and stipes of large fruitbodies but increased in the pilei. Changes in total amounts of these fractions show that gains by all fruitbodies during elongation exceeded the losses by the mycelium and that part of their nitrogen continues to be derived from the medium. Changes in 18 free and 17 protein amino acids were followed quantitatively in the colony. Free arginine, glutamic acid, ornithine, and alanine predominated in the mycelium and small fruitbodies during early growth of the latter, but arginine and ornithine decreased steeply thereafter. During rapid elongation of the large fruitbodies the concentration of arginine increased strongly in the pilei. The increase was much less in the stipes, but successive changes in the rest of the colony suggest that arginine is translocated into the large pilei from the mycelium and possibly the small fruitbodies. Aspartic and glutamic acids, leucine, and alanine predominated in protein of the whole colony until the early growth of fruitbodies, but protein composition changed during rapid elongation. The proportion of valine increased in the mycelium and it became the most abundant bound amino acid in large stipes. [14C]Leucine was fed in replacement medium and incorporation of the label was determined in nitrogenous fractions of different colony portions at the onset and termination of fruitbody growth. Most of the label transported into fruitbodies was in the ethanol-soluble free amino acids.

scholarly journals Proteinases from the Fruit-body of Flammulina velutipes.

1995 ◽  
Vol 42 (11) ◽  
pp. 907-912 ◽  
Author(s):  
Takao TERASHITA ◽  
Makoto NAWAMA ◽  
Kentaro YOSHIKAWA ◽  
Jiko SHISHIYAMA
Keyword(s):  
Fruit Body ◽  
Flammulina Velutipes

THE SOLUBLE PROTEINS OF THE MUSCLE TISSUE OF THE HADDOCK

1931 ◽  
Vol 6 (1) ◽  
pp. 1-11 ◽  
Author(s):  
J. F. LOGAN
Keyword(s):  
Sodium Chloride ◽  
Aqueous Solutions ◽  
Muscle Tissue ◽  
Soluble Protein ◽  
Potassium Phosphate ◽  
Extraction Methods ◽  
Water Soluble ◽  
Tabular Form ◽  
Water Soluble Protein ◽  
Isoelectric Points

As a contribution to the chemistry of muscle tissue, the solubility of the protein of haddock muscle in aqueous solutions of sodium chloride and neutral potassium phosphate, respectively, was determined. The results are expressed in tabular form and graphically in the form of solubility curves. A water-soluble protein and also a salt-soluble protein were isolated from dialyzed haddock muscle by extraction methods. These proteins were obtained in a comparatively pure condition by precipitation from solution in the region of their isoelectric points.

scholarly journals Separation and characterization of alkaline nuclease in the fruit body of Flammulina velutipes.

1985 ◽  
Vol 49 (7) ◽  
pp. 2181-2183 ◽  
Author(s):  
Shin''ichi KUROSAWA ◽  
Kazuharu KATOH ◽  
Hideki YOKOMICHI
Keyword(s):  
Fruit Body ◽  
Flammulina Velutipes ◽  
Alkaline Nuclease

FRACTIONATION OF LIVETIN AND THE MOLECULAR WEIGHTS OF THE α- AND β-COMPONENTS

1957 ◽  
Vol 35 (4) ◽  
pp. 241-250 ◽  
Author(s):  
W. G. Martin ◽  
J. E. Vandegaer ◽  
W. H. Cook
Keyword(s):  
Light Scattering ◽  
Soluble Protein ◽  
Soluble Fraction ◽  
Egg Yolk ◽  
Water Soluble ◽  
Water Soluble Fraction ◽  
Molecular Weights ◽  
Water Soluble Protein ◽  
Hen Egg Yolk ◽  
Hen Egg

Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.

Effect of Ginkgo Protein on Moisture Content and Hardness of Bread

2012 ◽  
Vol 531 ◽  
pp. 395-398
Author(s):  
Xiao Fei Sun ◽  
Yu Hui Qiao
Keyword(s):  
Moisture Content ◽  
Shelf Life ◽  
Total Protein ◽  
Soluble Protein ◽  
Water Soluble ◽  
Experimental Results ◽  
Water Soluble Protein

Ginkgo seeds were selected and used as experimental material to study protein compositions in ginkgo protein. Ginkgo protein was used as accessory to be added into flour to make bread. Effect of ginkgo protein on moisture content and hardness of bread were investigated. Experimental results showed that ginkgo protein contained water-soluble protein and salt-soluble protein which was 85.28 percents in total protein and contained small amounts of prolamin and alkali-soluble protein. The bread added with different ratios of ginkgo protein had higher moisture content and lower hardness. Therefore, adding appropriate amount of ginkgo protein could improve bread baking performances and bread shelf life.

scholarly journals Studies on silk proteins I. The properties and constitution of fibroin. The conversion of fibroin into a water-soluble form and its bearing on the phenomenon of denaturation

1947 ◽  
Vol 190 (1021) ◽  
pp. 145-169 ◽  
Keyword(s):  
Molecular Weight ◽  
Soluble Protein ◽  
Optical Rotation ◽  
Amino Nitrogen ◽  
Water Soluble ◽  
Soluble Form ◽  
Secondary Process ◽  
Amide Nitrogen ◽  
Water Soluble Protein ◽  
The Mean

Some of the constituent amino-acids of fibroin (degummed silk) are determined. Special attention is directed to histidine, owing to its use in the calculation of the molecular weight of fibroin. A value of 0⋅45% has been found by methods in which the histidine is isolated as nitranilate or di-(3:4-dichlorobenzenesulphonate). Other values obtained are serine 12⋅6%, threonine 1⋅5%, tyrosine 10⋅6%, and proline 1⋅5%. Hydroxyproline appears to be absent, but the presence of small amounts of some hydroxyamino-acid other than serine and threonine is indicated. The mean residue weight of fibroin is determined by three methods, one of which is a new method based on analysis of the complex formed between fibroin and cupri-ethylenediamine. This method gives a Cu:fibroin-N ratio of 1:1⋅92 and, if allowance is made for co-ordination with the tyrosine hydroxy1 group, an equivalence of 1⋅964 atoms of peptide-nitrogen to 1 atom of copper is obtained. The three methods give an average value of 78⋅0 for the mean residue weight of fibroin. This value, together with the most acceptable data for amino-acid constituents, indicate that the unidentified anhydro-residues (about 20%) have a mean residue weight of about 107. Evidence is presented that fibroin contains no amide-nitrogen. Methods for the determination of amide-nitrogen at present in use, which indicate a content of 1 to 2%, are considered to be unreliable. Fibroin dissolved in cupri-ethylenediamine gives, on neutralization and dialysis of the resulting solution, a water-soluble protein. The production of this water-soluble protein is attended by little or no degradation of the original fibroin as shown by determinations of fluidity, amino-nitrogen, and acid- and alkali-combining power. The water-soluble protein is precipitated by the normal protein-precipitating reagents, but in every instance examined the precipitated material exhibits an insolubility comparable with that of the original fibroin. Factors responsible for the solubilization process are investigated and data for molecular weight, titration values, ultra-violet absorption spectra, reducing activity, optical rotation, tryptic hydrolysis, and viscosity for both soluble and dispersed fibroin are given. Soluble fibroin has [ α ] D 15 — 53⋅1° and dispersed fibroin [ α ] D 15 — 58⋅9°, both in aqueous media. The preparation and properties of films and filaments of fibroin are described. Films of fibroin can be prepared that are water-soluble. On stretching, these films show strain-birefringence, acquire considerable tensile strength, and become insoluble in water, but X-ray examination gives the β -keratin pattern for both the stretched and unstretched films. Reasons are advanced for considering the water-soluble form of fibroin to be the native or renatured protein and the original protein to be the denatured form. The denaturation of fibroin is discussed on the basis that denaturation is essentially an unfolding of a coiled long-chain molecule. The subsequent aggregation of the uncoiled molecules to give an insoluble product is considered to be a secondary process. Some aspects of protein and polypeptide chains as macro-molecules are also discussed.

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