scholarly journals Enzymes of Aspergillus Oryzae I. The Development of a Culture Medium Yielding High Protease Activity

1952 ◽  
Vol 5 (1) ◽  
pp. 42 ◽  
Author(s):  
Margaret E Maxwell
Keyword(s):  
Ammonium Chloride ◽  
Aspergillus Oryzae ◽  
Protease Activity ◽  
Culture Medium ◽  
Invert Sugar ◽  
Rochelle Salt ◽  
Ammonium Tartrate ◽  
Sodium Potassium ◽  
Potassium Tartrate ◽  
High Protease Activity

When grown on modified Raulin's medium, containing additional sucrose, ammonium tartrate, and phosphate, Aspergillus oryzae yields more protease than when cultivated on unmodified Raulin's or Czapek-Dox media. Replacement of sucrose in the medium by fructose, invert sugar, glucose, maltose, starch, or lactose decreases the yield of enzyme in that order. Ammonium tartrate may be replaced by equivalent concentrations of the more readily available salts, sodium potassium tartrate (Rochelle salt) and ammonium chloride, without loss in activity.

Some anomalous optical properties of freshly-prepared mixed crystals of the Seignette salts

1924 ◽  
Vol 20 (104) ◽  
pp. 159-172 ◽  
Author(s):  
Harold E. Buckley
Keyword(s):  
Circular Polarization ◽  
Axial Plane ◽  
Continuous Series ◽  
Ammonium Tartrate ◽  
Crystalline Compound ◽  
Remarkable Property ◽  
Sodium Potassium ◽  
Sodium Potassium Tartrate ◽  
Potassium Tartrate ◽  
Rhombic System

The new crystalline compound triphenyl-bismuthine dichloride, described crystallographically by Mr. G. Greenwood (Min. Mag., 1923, vol. 20, p. 123), possesses the remarkable property of exhibiting crossed axial-plane dispersion of the rhombic ‘brookite’ type and circular polarization. For purposes of comparison, the author prepared specimens of the mixed Seiguette salts, which also exhibit crossed axial-plane dispersion together with circular polarization. The Seignette salts, sodium-potassium tartrate and sodium-ammonium tartrato, crystallize each with four molecules of water ill the bisphenoidal class of the rhombic system. They are truly isomorphous and form a continuous series of mixtures. The acute bisectrix for sodium-ammonium tartrate is normal to (001)and for sodium-potassium tartrate normal to (100). For all proportions of mixture containing 5 % and over of sodium-ammonium tartrate, the acute bisectrix is normal to (001).

scholarly journals The crystal structure of Rochelle salt (sodium potassium tartrate tetrahydrate NaKC 4 H 4 O 6 . 4H 2 O)

1941 ◽  
Vol 177 (969) ◽  
pp. 251-259 ◽  
Keyword(s):  
Crystal Structure ◽  
Carboxyl Groups ◽  
Water Molecules ◽  
Rochelle Salt ◽  
Sodium Potassium ◽  
Sodium Potassium Tartrate ◽  
Potassium Tartrate ◽  
Tetrahedral Bonding ◽  
Sodium And Potassium ◽  
Continuous Chain

The complete crystal structure of Rochelle salt (sodium potassium tartrate tetrahydrate) has been determined by Fourier and Patterson methods. Some of the difficulties in the application of these methods are discussed. The tartrate molecule is found to lie approximately in three planes, the planes of each half of the molecule being inclined at 60° to the plane of the carbon atoms. The tartrate molecules are bonded to sodium and potassium atoms both directly and through the medium of water molecules. If the water molecules are to preserve their customary tetrahedral ‘ bonding ’ it is necessary to suppose that one of the carboxyl groups of the molecule is also a dipole. A reversal of the continuous chain of carboxyl-water-water dipoles is a possible explanation of the peculiar dielectric properties of the salt.

scholarly journals Slow cooling of protein crystals

2009 ◽  
Vol 42 (5) ◽  
pp. 944-952 ◽  
Author(s):  
Matthew Warkentin ◽  
Robert E. Thorne
Keyword(s):  
Ice Nucleation ◽  
Glycerol Solution ◽  
X Ray Diffraction ◽  
Slow Cooling ◽  
Sodium Potassium ◽  
X Ray ◽  
Structure And Dynamics ◽  
Potassium Tartrate ◽  
Flash Cooling ◽  
Diffraction Patterns

Cryoprotectant-free thaumatin crystals have been cooled from 300 to 100 K at a rate of 0.1 K s−1– 103–104times slower than in conventional flash cooling – while continuously collecting X-ray diffraction data, so as to follow the evolution of protein lattice and solvent properties during cooling. Diffraction patterns show no evidence of crystalline ice at any temperature. This indicates that the lattice of protein molecules is itself an excellent cryoprotectant, and with sodium potassium tartrate incorporated from the 1.5 Mmother liquor ice nucleation rates are at least as low as in a 70% glycerol solution. Crystal quality during slow cooling remains high, with an average mosaicity at 100 K of 0.2°. Most of the mosaicity increase occurs above ∼200 K, where the solvent is still liquid, and is concurrent with an anisotropic contraction of the unit cell. Near 180 K a crossover to solid-like solvent behavior occurs, and on further cooling there is no additional degradation of crystal order. The variation ofBfactor with temperature shows clear evidence of a protein dynamical transition near 210 K, and at lower temperatures the slope dB/dTis a factor of 3–6 smaller than has been reported for any other protein. These results establish the feasibility of fully temperature controlled studies of protein structure and dynamics between 300 and 100 K.

scholarly journals Enhancement of Acid Protease Activity of Aspergillus oryzae Using Atmospheric and Room Temperature Plasma

2020 ◽  
Vol 11 ◽  
Author(s):  
Liang Shu ◽  
Xiaoguang Si ◽  
Xinda Yang ◽  
Wenyan Ma ◽  
Jinglan Sun ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Protease Activity ◽  
Room Temperature ◽  
Acid Protease ◽  
Temperature Plasma

Use of cell cultures to differentiate among effects of various ischemia factors on astrocytic cell volume

1992 ◽  
Vol 70 (S1) ◽  
pp. S344-S349 ◽  
Author(s):  
Bernhard H. J. Juurlink ◽  
Ye Chen ◽  
Leif Hertz
Keyword(s):  
Cell Volume ◽  
Cell Cultures ◽  
Culture Medium ◽  
In Vitro Models ◽  
Similar Amount ◽  
Sodium Potassium ◽  
Astrocytic Swelling ◽  
Per Se ◽  
Substrate Deprivation

Mouse astrocytes were subjected to in vitro models of ischemia (hypoxia with or without substrate deprivation, excess potassium, or elevated glutamate). Three hours of hypoxia alone or with substrate deprivation had little effect upon the morphology of astrocytes but did cause disaggregation of polyribosomes. Excess (12–50 mM) potassium added (as KCl) to a normal isotonic medium also caused no swelling; it did, however, cause a shrinkage of cell volume. When 50 mM potassium was substituted for a similar amount of sodium, marked swelling occurred. Swelling of astrocytes was also seen after addition of glutamate (50 μM to 1 mM) to the culture medium. These results show that ischemia per se does not result in astrocytic swelling; rather, microenvironmental alterations such as rising glutamate levels and changes in the sodium/potassium ratios result in astrocytic swelling. We conclude that one can use astrocytes in culture to dissect out the mechanisms that cause postischemic alterations in astrocytes in vivo.Key words: astrocytes, glutamate, ischemia, potassium, swelling.

scholarly journals Canola Cake as a Potential Substrate for Proteolytic Enzymes Production by a Selected Strain of Aspergillus oryzae: Selection of Process Conditions and Product Characterization

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Adriana C. Freitas ◽  
Ruann J. S. Castro ◽  
Maria A. Fontenele ◽  
Antonio S. Egito ◽  
Cristiane S. Farinas ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Protease Activity ◽  
Incubation Temperature ◽  
Initial Conditions ◽  
Proteolytic Enzymes ◽  
Inoculum Size ◽  
Protease Production ◽  
Process Conditions ◽  
Enzymatic Extract ◽  
Technological Advances

Oil cakes have excellent nutritional value and offer considerable potential for use in biotechnological processes that employ solid-state fermentation (SSF) for the production of high value products. This work evaluates the feasibility of using canola cake as a substrate for protease production by a selected strain of Aspergillus oryzae cultivated under SSF. The influences of the following process parameters were considered: initial substrate moisture content, incubation temperature, inoculum size, and pH of the buffer used for protease extraction and activity analysis. Maximum protease activity was obtained after cultivating Aspergillus oryzae CCBP 001 at 20°C, using an inoculum size of 107 spores/g in canola cake medium moistened with 40 mL of water to 100 g of cake. Cultivation and extraction under selected conditions increased protease activity 5.8-fold, compared to the initial conditions. Zymogram analysis of the enzymatic extract showed that the protease molecular weights varied between 31 and 200 kDa. The concentrated protease extract induced clotting of casein in 5 min. The results demonstrate the potential application of canola cake for protease production under SSF and contribute to the technological advances needed to increase the efficiency of processes designed to add value to agroindustrial wastes.

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