Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus

Min Jen Tseng; Mee-Ngan Frances Yap; Khanok Ratanakhanokchai; Khin Lay Kyu; Shui Tein Chen

doi:10.1016/S0141-0229(02)00018-2

Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus

Min Jen Tseng^*, Mee-Ngan Frances Yap, Khanok Ratanakhanokchai, Khin Lay Kyu, Shui Tein Chen

^*Corresponding author for this work

Microbiology-Immunology

Research output: Contribution to journal › Article › peer-review

70 Scopus citations

Abstract

Two xylanases from Bacillus firmus were purified to homogeneity by gel filtration and ion-exchange chromatography. These enzymes have molecular weights of 45 kDa and 23 kDa, respectively, and both show enzymatic activity over the pH range of 5.0-11.0 at 37°C. These enzymes hydrolyzed xylan from birchwood to release mainly the products of xylose, xylotriose and xylohexose, thus indicating that the xylanases act preferentially toward the internal glycosidic bonds of xylo-oligosaccharides. However, the two xylanases show different modes of action, and a combination of both is likely to lead to concerted degradation of xylan down to the mono- and disaccharides.

Original language	English (US)
Pages (from-to)	590-595
Number of pages	6
Journal	Enzyme and Microbial Technology
Volume	30
Issue number	5
DOIs	https://doi.org/10.1016/S0141-0229(02)00018-2
State	Published - May 2 2002

Funding

We thank Dr. G. Robert Greenberg for insightful comments of this manuscript. This work was supported by National Science Council of Taiwan (to M.-J. T., S.-T. C.) and Taipei Medical University (to M.-J. T.).

Keywords

Bacillus firmus
Enzyme purification
Xylanase action
Xylanases

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biochemistry
Applied Microbiology and Biotechnology

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10.1016/S0141-0229(02)00018-2

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title = "Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus",

abstract = "Two xylanases from Bacillus firmus were purified to homogeneity by gel filtration and ion-exchange chromatography. These enzymes have molecular weights of 45 kDa and 23 kDa, respectively, and both show enzymatic activity over the pH range of 5.0-11.0 at 37°C. These enzymes hydrolyzed xylan from birchwood to release mainly the products of xylose, xylotriose and xylohexose, thus indicating that the xylanases act preferentially toward the internal glycosidic bonds of xylo-oligosaccharides. However, the two xylanases show different modes of action, and a combination of both is likely to lead to concerted degradation of xylan down to the mono- and disaccharides.",

keywords = "Bacillus firmus, Enzyme purification, Xylanase action, Xylanases",

author = "Tseng, {Min Jen} and Yap, {Mee-Ngan Frances} and Khanok Ratanakhanokchai and Kyu, {Khin Lay} and Chen, {Shui Tein}",

note = "Funding Information: We thank Dr. G. Robert Greenberg for insightful comments of this manuscript. This work was supported by National Science Council of Taiwan (to M.-J. T., S.-T. C.) and Taipei Medical University (to M.-J. T.).",

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T1 - Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus

AU - Tseng, Min Jen

AU - Yap, Mee-Ngan Frances

AU - Ratanakhanokchai, Khanok

AU - Kyu, Khin Lay

AU - Chen, Shui Tein

N1 - Funding Information: We thank Dr. G. Robert Greenberg for insightful comments of this manuscript. This work was supported by National Science Council of Taiwan (to M.-J. T., S.-T. C.) and Taipei Medical University (to M.-J. T.).

PY - 2002/5/2

Y1 - 2002/5/2

N2 - Two xylanases from Bacillus firmus were purified to homogeneity by gel filtration and ion-exchange chromatography. These enzymes have molecular weights of 45 kDa and 23 kDa, respectively, and both show enzymatic activity over the pH range of 5.0-11.0 at 37°C. These enzymes hydrolyzed xylan from birchwood to release mainly the products of xylose, xylotriose and xylohexose, thus indicating that the xylanases act preferentially toward the internal glycosidic bonds of xylo-oligosaccharides. However, the two xylanases show different modes of action, and a combination of both is likely to lead to concerted degradation of xylan down to the mono- and disaccharides.

AB - Two xylanases from Bacillus firmus were purified to homogeneity by gel filtration and ion-exchange chromatography. These enzymes have molecular weights of 45 kDa and 23 kDa, respectively, and both show enzymatic activity over the pH range of 5.0-11.0 at 37°C. These enzymes hydrolyzed xylan from birchwood to release mainly the products of xylose, xylotriose and xylohexose, thus indicating that the xylanases act preferentially toward the internal glycosidic bonds of xylo-oligosaccharides. However, the two xylanases show different modes of action, and a combination of both is likely to lead to concerted degradation of xylan down to the mono- and disaccharides.

KW - Bacillus firmus

KW - Enzyme purification

KW - Xylanase action

KW - Xylanases

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U2 - 10.1016/S0141-0229(02)00018-2

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VL - 30

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EP - 595

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 5

ER -

Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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