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.

Production and Properties of a Bacterial Thermostable Exo-inulinase

2001 ◽  
Vol 56 (11-12) ◽  
pp. 1022-1028 ◽  
Author(s):  
Kristina Uzunova ◽  
Anna Vassileva ◽  
Margarita Kambourova ◽  
Viara Ivanova ◽  
Dimitrina Spasova ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Enzyme Preparation ◽  
Batch Cultivation ◽  
Crude Enzyme ◽  
Growth Time ◽  
Bacillus Sp ◽  
High Thermostability ◽  
Crude Enzyme Preparation ◽  
Ph Range

Abstract Enzyme production of newly isolated thermophilic inulin-degrading Bacillus sp. 11 strain was studied by batch cultivation in a fermentor. The achieved inulinase and invertase activi­ ties after a short growth time (4.25 h) were similar or higher compared to those reported for other mesophilic aerobic or anaerobic thermophilic bacterial producers and yeasts. The investigated enzyme belonged to the exo-type inulinases and splitted-off inulin, sucrose and raffinose. It could be used at temperatures above 65 °C and pH range 5.5-7.5. The obtained crude enzyme preparation possessed high thermostability. The residual inulinase and inver­ tase activities were 92-98% after pretreatment at 65 °C for 60 min in the presence of substrate inulin.

Two types of xylanases of alkalophilic Bacillus sp. No. C-125

1985 ◽  
Vol 31 (6) ◽  
pp. 538-542 ◽  
Author(s):  
H. Honda ◽  
T. Kudo ◽  
Y. Ikura ◽  
K. Horikoshi
Keyword(s):  
Ammonium Sulfate ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Bacillus Sp ◽  
Ammonium Sulfate Precipitation ◽  
Molecular Weights ◽  
Protein Molecules ◽  
Activity Curve ◽  
Alkalophilic Bacillus ◽  
Hydrolysis Of

One alkalophilic Bacillus sp. strain C-125 (FERM No. 7344) was isolated from soil. From this organism, two types of xylanases, designated xylanase A and xylanase N, were purified by an ammonium sulfate precipitation followed by Biogel P-30 gel filtration, DEAE-cellulose chromatography, and Sephadex G-75 gel filtration. The molecular weights of xylanase A and N were estimated as 43 000 and 16 000, respectively. Immunological experiments indicated that xylanase A and xylanase N were entirely different protein molecules. Xylanase N was most active at pH 6.0–7.0, but xylanase A had a very broad pH activity curve (pH 6–10) and was still active even at pH 12.0. The maximum hydrolysis of xylan by the enzymes was about 25%. Both enzymes split xylan and yielded xylobiose and higher oligosaccharides but could hydrolyze neither xylobiose nor xylotriose. Trans xylosidation activities were detected in both enzymes.

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.

scholarly journals Pretreatment of pectic wastewater with pectate lyase from an alkalophilic Bacillus sp.

1988 ◽  
Vol 52 (7) ◽  
pp. 1855-1856 ◽  
Author(s):  
Hiroyuki TANABE ◽  
Yoshinari KOBAYASHI ◽  
Isao AKAMATSU
Keyword(s):  
Pectate Lyase ◽  
Bacillus Sp ◽  
Alkalophilic Bacillus

scholarly journals Nucleotide Sequence of the Xylanase A Gene of Alkalophilic Bacillus sp. Strain C-125

1987 ◽  
Vol 51 (3) ◽  
pp. 953-955
Author(s):  
Tetsuo Hamamoto ◽  
Hiroshi Honda ◽  
Toshiaki Kudo ◽  
Koki Horikoshi
Keyword(s):  
Nucleotide Sequence ◽  
Bacillus Sp ◽  
Alkalophilic Bacillus
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