Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23

Abstract

BLANCO, A., and PASTOR, F.I.J. 1993. Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23. Can. J. Microbiol. 39: 1162-1166. A Bacillus strain with xylanase activity has been isolated. Maximum xylanase production was obtained when the strain was cultured in media supplemented with birchwood xylan or rice straw; production was repressed by glucose and xylose. The optimal temperature and pH for xylanase activity were 4550°C and 5.5-7.5, respectively. Crude xylanase was highly stable at a wide range of pH values, retaining 100070 of the activity after 24 h of incubation at 37°C in buffer at pH 10.0. Analysis by polyacrylamide gel electrophoresis and zymogram techniques showed four xylanase activity bands with apparent molecular masses of 32, 48, 61, and 66 kDa. The most active of them (molecular mass 32 kDa) apparently corresponded to a xylanase with an isoelectric point (PI) of 9.3 in isoelectrofocusing gels developed as zymograms. Four other bands with xylanase activity were detected at pIs of 7.7, 5.6, 5.0, and 4.5. Analysis for carboxymethylcellulase activity revealed that only the band of 48 kDa and the band with a pI of 7.7 showed hydrolytic activity against the cellulosic substrate.

Microbial diversity in the larval gut of field and laboratory populations of the sugarcane weevil Sphenophorus levis (Coleoptera, Curculionidae)

“…Microorganisms from the Paenibacillus genus were isolated from laboratory larvae; this was the most abundant group of organisms to present CMCase activity. The strain Paenibacillus sp BP-23 (formerly Bacillus sp BP-23) (Blanco and Pastor, 1993) has been reported to have a multi-enzymatic glucanase system, including several cellulases (Pastor et al, 2001) and xylanases (Blanco et al, 1999). Several cellulolytic microorganisms were found in both populations, although the highest cellulolytic activity was observed in bacteria isolated from the laboratory population.…”

An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization The EMBL accession number for the nucleotide sequence determined in this work is AJ237980.

“…strain BP-23 was isolated from soil from a rice field in the Ebro river delta (Blanco & Pastor, 1993) and has been deposited in the Spanish 0002-3615 # 2000 SGM Type Culture Collection as strain CECT 4592. The strain was grown as described previously (Blanco & Pastor, 1993). Escherichia coli 5K (Godessart et al, 1988) was used as the recipient strain for recombinant plasmids.…”

“…BP-23, previously isolated from an enrichment culture on rice straw, secretes a complex system of carbohydrate-degrading enzymes including pectinases (Blanco & Pastor, 1993). The influence of carbon sources on pectate lyase production by the strain was evaluated.…”

“…The strain Bacillus sp. BP-23, previously isolated from a rice field (Blanco & Pastor, 1993), shows a multiple glycanase system, some enzymes of which have been cloned and characterized (Blanco et al, 1995(Blanco et al, , 1998(Blanco et al, , 1999. In this article, we describe the cloning and characterization of pectate lyase A from Bacillus sp.…”

Exo‐mode of action of cellobiohydrolase Cel48C from Paenibacillus sp. BP‐23

“…BP-23 (formerly Bacillus sp. BP-23) [19] shows a multienzymatic glycanase system, including several cellulases [20,21], xylanases [22,23], or pectinases [24]. In this study we report the cloning, purification and characterization of Paenibacillus sp.…”