scholarly journals Fungal Cellulases II. The Complexity of Enzymes from Aspergillus Oryzae that Split ,ß-Glucosidic Linkages, and their Partial Separation

1952 ◽  
Vol 5 (4) ◽  
pp. 433 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Aspergillus Oryzae ◽  
Paper Chromatography ◽  
Filter Paper ◽  
Carboxymethyl Cellulose ◽  
Enzyme Preparation ◽  
Paper Electrophoresis ◽  
Sodium Carboxymethyl Cellulose ◽  
Component Mixture ◽  
Crude Enzyme Preparation ◽  
Two Component

Filter paper electrophoresis and paper chromatography have been used to test the homogeneity of the ,8-glucosidase of Aspergillus oryzae. In the crude enzyme preparation there are at least eight components capable of breaking ,8-glucosidic linkages and showing varying degrees of specificity towards different substrates. These are active not only in splitting simple glucosides but also in depolymerizing sodium carboxymethyl cellulose. The only exception is provided by the enzymes splitting p-nitrophenyl-,8-glucoside, wWch are sharply limited to two closely related components. TWs two-component mixture has been partially purified from accompanying enzymes.

Cellulases of an alkalophilic Bacillus strain isolated from soil

1984 ◽  
Vol 30 (6) ◽  
pp. 774-779 ◽  
Author(s):  
K. Horikoshi ◽  
M. Nakao ◽  
Y. Kurono ◽  
N. Sashihara
Keyword(s):  
Carboxymethyl Cellulose ◽  
Enzyme Preparation ◽  
Bacillus Sp ◽  
Bacillus Pasteurii ◽  
Crude Enzyme Preparation ◽  
Cmcase Activity ◽  
Multienzyme System ◽  
Activity Curve ◽  
Alkalophilic Bacillus ◽  
Optimal Ph

A cellulolytic alkalophile, Bacillus sp. No. N-4, was isolated from soil and found to be similar to Bacillus pasteurii, except for its ability to grow at high pH. The isolate grew well at a pH ranging from about 8 to 11 and was a good producer of carboxymethyl cellulase (CMCase) activity, which was associated with a multienzyme system. The crude enzyme preparation strongly hydrolyzed carboxymethyl cellulose and had a broad pH activity curve (pH 5–10). Two alkaline CMCases (enzyme E1 and E2) having an optimal pH for enzyme action at pH 10.0 were partially purified. The enzyme E2 was stable up to 80 °C, and E1 up to 60 °C. Both enzymes hydrolyzed cellotetraose and preferentially yielded cellobiose.

Fungal Cellulases I. General Properties of Unpurified Enzyme Preparations From Aspergillus Oryz.A'e

1952 ◽  
Vol 5 (4) ◽  
pp. 409 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Carbon Source ◽  
Aspergillus Oryzae ◽  
Culture Filtrate ◽  
Carboxymethyl Cellulose ◽  
Sodium Carboxymethyl Cellulose ◽  
Enzyme Preparations ◽  
General Properties

The culture filtrate from Aspergillus oryzae contains enzymes capable of depolymerizing sodium carboxymethyl cellulose (SCMC) and of splitting all ,B-glucosides tested. These enzymes are produced by the mould in the absence of cellulose or any other carbon source containing ,B-glucosidic linkages

Fifth virial coefficient of a two-component mixture of hard discs

1997 ◽  
Vol 90 (4) ◽  
pp. 679-681
Author(s):  
F. SAIJA ◽  
G. FIUMARA ◽  
P.V. GIAQUINTA
Keyword(s):  
Virial Coefficient ◽  
Component Mixture ◽  
Two Component

Effects of Trehalose and Sodium Carboxymethyl Cellulose on Prevention of Organ Adhesion after Laparotomy: A Preliminary Study

2009 ◽  
Vol 40 (2) ◽  
pp. 19-26 ◽  
Author(s):  
Soojung LEE ◽  
Yasutsugu MIWA ◽  
Ryohei NISHIMURA ◽  
Ung-il CHUNG ◽  
Shigeki SUZUKI ◽  
...  
Keyword(s):  
Carboxymethyl Cellulose ◽  
Sodium Carboxymethyl Cellulose ◽  
Preliminary Study

Optimization of hydroxypropyl methylcellulose and sodium carboxymethyl cellulose in buccal film salbutamol sulphate

2020 ◽  
Vol 23 (03) ◽  
pp. 33-49
Author(s):  
Ni’matul Mauludiyah ◽  
Devi Ayu Aprillia ◽  
Viddy Agustian Rosyidi ◽  
Lusia Oktora Ruma Kumala Sari
Keyword(s):  
Carboxymethyl Cellulose ◽  
Hydroxypropyl Methylcellulose ◽  
Sodium Carboxymethyl Cellulose ◽  
Salbutamol Sulphate

Cholesterol in Serum and Lipoprotein Fractions

1956 ◽  
Vol 2 (3) ◽  
pp. 145-159 ◽  
Author(s):  
Joseph T Anderson ◽  
Ancel Keys
Keyword(s):  
Human Serum ◽  
Total Cholesterol ◽  
Filter Paper ◽  
Room Temperature ◽  
Paper Electrophoresis ◽  
Cholesterol Content ◽  
Intraindividual Variability ◽  
Detailed Data ◽  
The Stability ◽  
Source Of Error

Abstract 1. Methods are described for the separation, by paper electrophoresis and by cold ethanol, of α- and β-lipoproteins in 0.1 ml. of serum, with subsequent analysis of cholesterol in the separated portions. 2. It is shown that both methods of separation yield separated fractions containing substantially the same amounts of cholesterol. 3. Detailed data are given on the errors of measurement for total cholesterol and for cholesterol in the separated lipoprotein fractions. 4. Studies are reported on the stability of cholesterol in stored serum and on paper electrophoresis strips. It is shown that simple drying on filter paper causes no change in cholesterol content and yields a product that is stable for many weeks at ordinary room temperature. 5. The sources of variability in human serum cholesterol values are examined and it is shown that spontaneous intraindividual variability is a much greater source of error than the errors of measurement with these methods.

Sign in / Sign up

Export Citation Format

Share Document