An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization

Article Abstract:

Results demonstrate that pelA gene from Bacillus sp. BP-23 encodes a 23 kDa protein which exhibited homology to bacterial pectate lyases. Data show the enzyme depolymerizes polygalacturonate and pectins with optimal activity at pH 10 and 50 C temperature.

Spain, Statistical Data Included, Usage, Physiological aspects, Pectin, Cloning

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Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23

Article Abstract:

The bacillus strain BP-23 produces xylanase A, which has a molecular mass of 32 kDa and an isoelectric point of 9.3. The enzyme's activity is maximum at 50 degree celsius and a pH of 5.5. It is also active at alkaline pHs. N-bromosuccinimide suppresses xylanase activity. Incubation of birchwood bark pulp with xylanase A increases the bleachability of pulp and decreases chlorine dioxide consumption by 38%. The amino-terminal sequence of xylanase A has a conserved sequence of five amino acids.

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A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

Article Abstract:

The cloning and sequencing of the gene encoding xylanase C from Bacillus sp BP-23 and the characterization of the enzyme are described. The enzyme XynC discussed is the only xylanase from Bacillus spp that exhibits a multidomain structure with three independent domains. It shows a family IX cellulose-binding domain and a region homologous to thermostabilizing domains. Therefore, Xyn C is unique since it is the only example of an enzyme from the genus Bacillus demonstrating these types of domains.

Bacterial proteins

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