Purification and characterization of a new xylanase (xylanase B) produced by Streptomyces lividans 66

Abstract

A new extracellular xylanase produced by Streptomyces lividans 66 was isolated from a genetically engineered clone of that strain. This enzyme, named xylanase B, has an Mr of 31,000 and acts specifically on xylan as an endo-type xylanase producing short-chain xylo-oligosaccharides. The activity is optimal at pH 6.5 and at a temperature of 55 degrees C, which is similar to that of the previously characterized xylanase A. Xylanase B is glycosylated and has a pI of 8.4; its Km and Vmax. values are 3.71 mg/ml and 1.96 mmol/mg of enzyme respectively. Specific antibodies raised against xylanase A show no cross-reaction with xylanase B; however, the anti-(xylanase B) antibodies react slightly with xylanase A. A comparison of the hydrolysis products obtained from oat-spelts xylan with both enzymes show that xylanase A preferentially degrades short-chain oligo-xylosides, whereas xylanase B acts on the longer, water-insoluble, molecules.

Gene Cloning, Expression, and Characterization of a Thermostable Xylanase from Nesterenkonia xinjiangensis CCTCC AA001025

“…This xylanase had high sequence homology to the xylanases from Actinomycetes, but showed much broader pH adaptability and higher thermostability. For example, STX-II from S. thermoviolaceus OPC-520 and the xylanase B from S. lividans 66 had similar pH optima at 7.0 and 6.5, respectively, but showed almost no activity when assayed at pH below 4.0 or above 9.0 [15,19]. Some xylanases have similar optimal temperature at 55°C as Xyn11NX did, such as Xys1L from S. halstedii JM8 [16] and SfXyn10 from S. fradiae var.…”

“…AR-135 [14], S. thermoviolaceus OPC-520 [15], Streptomyces halstedii JM8 [16], Streptomyces fradiae var. k11 [17], Nonomuraea flexuosa [18], Streptomyces lividans 66 [19], and so on. In this study, we first described cloning and expression of a family 11 xylanase, Xyn11NX, from the genus Nesterenkonia.…”

The xylan-degrading enzyme system of Talaromyces emersonii: novel enzymes with activity against aryl β-d-xylosides and unsubstituted xylans

“…Xylanases can also hydrolyse higher xylo-oligosaccharides, the affinity for such substrates increasing with increasing degree of polymerization (DP) [2,3]. By contrast with the ,-xylosidases, they do not cleave xylobiose and most such enzymes investigated, including representatives from Aspergillus niger [9], Aspergillus ochraeus [10], Bacillus subtilis [11], Humicola grisea var thermoidea [12] and Streptomyces lividans [13,14], do not hydrolyse arylf-D-xylosides. Again, however, some exceptions have been noted.…”

Optimization of Cellulase-Free Xylanase Production by Thermophilic Streptomyces thermovulgaris TISTR1948 through Plackett-Burman and Response Surface Methodological Approaches

“…The oligosaccharides are digested at the non-reducing ends by -D-xyloxidases to xylose as well asglucuronidases (EC 3.2.1.139), acetylxylan esterase (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), and even -L-arabinofuranosidases (EC 3.2.1.55). 3) There are many reports on xylanase production by microorganisms such as Streptomyces lividans 66, 4) Bacillus pumilus, 5) Thermoascus aurantiacus, 6) Streptomyces sp. Ab106, 7,8) Paecilomyces thermophila, 9) Bacillus sp.…”