Purification and Characterization of Thermostable Endo-1,5-α- l -Arabinase from a Strain of Bacillus thermodenitrificans
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چکیده
منابع مشابه
Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1
This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...
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Isolation of novel thermophilic bacilli has received considerable attention among the scientific community in whole world because of their biotechnological importance as they possess unique enzymes with thermal activity and stability. Of the thermophilic enzymes, we were interested in α-glucosidases which catalyze hydrolysis of terminal non-reducing α-D-glucosidic linkages of oligoand polysacch...
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Background: Pectinases are pectin degrading class of enzymes including polygalacturonase (PG), polymethyl galacturonase (PMG), pectate lyase (PEL), and pectin esterase (PE) that are commonly used in processes involving the degradation of plant materials, such as speeding up the extraction of fruit juices. Objectives: A highly methylated pectin degrading bacterium from soil covered with fruit wa...
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متن کاملTwo-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis
The aim of this study was production and partial purification of α-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37 °C and pH 7.0. The α-amylase enzyme was purified by ion exchange chromatography ...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2002
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.68.4.1639-1646.2002