Cohnella sp. A01 laccase: thermostable, detergent resistant, anti-environmental and industrial pollutants enzyme
نویسندگان
چکیده
منابع مشابه
Thermostable chitinase from Cohnella sp. A01: isolation and product optimization
Twelve bacterial strains isolated from shrimp farming ponds were screened for their growth activity on chitin as the sole carbon source. The highly chitinolytic bacterial strain was detected by qualitative cup plate assay and tentatively identified to be Cohnella sp. A01 based on 16S rDNA sequencing and by matching the key morphological, physiological, and biochemical characteristics. The culti...
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Background: Typically, non-cellulytic glucanase, including fungi and yeast cell wall hydrolyzing enzymes, are released by some symbiotic fungi and plants during the mycoparasitic fungi attack on plants. These enzymes are known as the defense mechanisms of plants. This study intends to investigate the biochemical properties of β-1,6-glucanase (bg16M) from native thermophilic bacteria, Cohne...
متن کاملProduction and industrial applications of laccase enzyme
Laccase is an enzyme that has potential ability of oxidation. It belongs to those enzymes, which have innate properties of reactive radical production, and its utilization in many fields has been ignored because of its unavailability in the commercial field. There are diverse sources of laccase producing organisms like bacteria, fungi and plants. Textile, pulp and paper industries discharge a h...
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A Gram-positive, rod-shaped, endospore-forming organism, strain CCUG 47242T, was isolated from a sample of industrial starch production in Sweden. 16S rRNA gene sequence analysis demonstrated that this isolate was moderately related to species of the genus Paenibacillus, with <94.4 % sequence similarity to all other hitherto described Paenibacillus species. Strain CCUG 47242T showed the greates...
متن کاملPurification and Characterization of Thermostable and Detergent-Stable α-Amylase from Anoxybacillus sp. AH1.
A thermostable and detergent-stable α-amylase from a newly isolated Anoxybacillus sp. AH1 was purified and characterized. Maximum enzyme production (1874.8 U/mL) was obtained at 24 h of incubation. The amylase was purified by using Sephadex G-75 gel filtration, after which an 18-fold increase in specific activity and a yield of 9% were achieved. The molecular mass of the purified enzyme was est...
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ژورنال
عنوان ژورنال: Heliyon
سال: 2019
ISSN: 2405-8440
DOI: 10.1016/j.heliyon.2019.e02543