Purification and properties of a xylan-binding endoxylanase from Alkaliphilic bacillus sp. strain K-1.

Purification and Properties of a Xylan-Binding Endoxylanase from Alkaliphilic Bacillus sp. Strain K-1 KHANOK RATANAKHANOKCHAI,* KHIN LAY KYU, AND MORAKOT TANTICHAROEN

A calcium-dependent xylan-binding domain of alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1.

Xylanase J of alkaliphilic Bacillus sp. strain 41M-1 contains a carbohydrate-binding module family 36 xylan-binding domain (XBD). Mutational analysis of the XBD revealed that Tyr237, Asp313, Trp317, and Asp318 were involved in Ca(2+)-dependent xylan-binding, and that Asp313 and Asp318 were especially important.

Purification of Endoxylanase from Bacillus pumilus B20 for Production of Prebiotic Xylooligosaccharide Syrup; An In vitro Study

Background: The need for more cost-effective compounds is imperative because the demand for prebiotic compounds is ever on the rise. Objective: The focus of this study is the purification of the endoxylanase from Bacillus pumilus B20 and its application in a cost-effective production of the prebiotic xylooligosaccharide (XOS) syrup having a high concentration of oligo...

Global Microarray Analysis of Carbohydrate Use in Alkaliphilic Hemicellulolytic Bacterium Bacillus sp. N16-5

The alkaliphilic hemicellulolytic bacterium Bacillus sp. N16-5 has a broad substrate spectrum and exhibits the capacity to utilize complex carbohydrates such as galactomannan, xylan, and pectin. In the monosaccharide mixture, sequential utilization by Bacillus sp. N16-5 was observed. Glucose appeared to be its preferential monosaccharide, followed by fructose, mannose, arabinose, xylose, and ga...

Purification and some properties of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1.

A novel alkaliphilic Nocardiopsis sp., strain TOA-1, was isolated from a tile-joint of a bathroom. Strain TOA-1 produced a variety of alkaline hydrolytic enzymes. An alkaline protease, designated NAPase, was purified and characterized. NAPase had a very high keratinolytic activity and high stability under acidic conditions.