Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116

Min Soo Kim, Mi Hee Woo, Young Hyo Chang, Namhyun Chung, Joong Su Kim

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

In our present study, a new Endo-1,4-β-xylanase (EC 3.2.1.8) was isolated, which belongs to glycosyl hydrolase family 10 member. The new enzyme designated as xynA was expressed for biochemical characterization. The xynA xylanase was identified in Paenibacillus sp. EC116. The novel gene had the size of 2673 base pairs, which correspond to 891 amino acid residues. The expressed enzyme has a size of ~100 kDa. The amino acid sequence was similar to that of endo-1,4-beta-xylanase from Paenibacillus sp. FSL R5-192 (ETT36211.1) (96 % identical). The xylanase has an optimal temperature of 40 °C and the pH optimum of 6.0. The specific activity of the xylanase toward birchwood xylan was about 0.69 μmol min−1 mg−1, the Vmax value of 1.639 μmol mg−1 min−1, and the Km value of 35.1 mg ml−1. The EC116 xylanase was relatively stable up to 60 °C. Xylanase enzymes have numerous industrial applications, which need to meet the specific requirements for each application. We hope that our EC116 xylanase is one of the candidates for commercial applications.

Original languageEnglish
Pages (from-to)313-320
Number of pages8
JournalApplied Biological Chemistry
Volume59
Issue number2
DOIs
Publication statusPublished - 2016 Apr 1

Fingerprint

Paenibacillus
Enzymes
Endo-1,4-beta Xylanases
Amino Acids
Xylans
Hydrolases
Base Pairing
Industrial applications
Amino Acid Sequence
Genes
Temperature

Keywords

  • Glycosyl hydrolase family 10
  • Paenibacillus sp
  • Saccharification
  • Xylanase
  • Β-glucosidase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Organic Chemistry

Cite this

Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116. / Kim, Min Soo; Woo, Mi Hee; Chang, Young Hyo; Chung, Namhyun; Kim, Joong Su.

In: Applied Biological Chemistry, Vol. 59, No. 2, 01.04.2016, p. 313-320.

Research output: Contribution to journalArticle

Kim, Min Soo ; Woo, Mi Hee ; Chang, Young Hyo ; Chung, Namhyun ; Kim, Joong Su. / Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116. In: Applied Biological Chemistry. 2016 ; Vol. 59, No. 2. pp. 313-320.
@article{e776cd5a14bc4efe901e59d72157b592,
title = "Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116",
abstract = "In our present study, a new Endo-1,4-β-xylanase (EC 3.2.1.8) was isolated, which belongs to glycosyl hydrolase family 10 member. The new enzyme designated as xynA was expressed for biochemical characterization. The xynA xylanase was identified in Paenibacillus sp. EC116. The novel gene had the size of 2673 base pairs, which correspond to 891 amino acid residues. The expressed enzyme has a size of ~100 kDa. The amino acid sequence was similar to that of endo-1,4-beta-xylanase from Paenibacillus sp. FSL R5-192 (ETT36211.1) (96 {\%} identical). The xylanase has an optimal temperature of 40 °C and the pH optimum of 6.0. The specific activity of the xylanase toward birchwood xylan was about 0.69 μmol min−1 mg−1, the Vmax value of 1.639 μmol mg−1 min−1, and the Km value of 35.1 mg ml−1. The EC116 xylanase was relatively stable up to 60 °C. Xylanase enzymes have numerous industrial applications, which need to meet the specific requirements for each application. We hope that our EC116 xylanase is one of the candidates for commercial applications.",
keywords = "Glycosyl hydrolase family 10, Paenibacillus sp, Saccharification, Xylanase, Β-glucosidase",
author = "Kim, {Min Soo} and Woo, {Mi Hee} and Chang, {Young Hyo} and Namhyun Chung and Kim, {Joong Su}",
year = "2016",
month = "4",
day = "1",
doi = "10.1007/s13765-016-0159-6",
language = "English",
volume = "59",
pages = "313--320",
journal = "Applied Biological Chemistry",
issn = "2468-0834",
publisher = "Springer Netherlands",
number = "2",

}

TY - JOUR

T1 - Biochemical characterization of a noble xylanase from Paenibacillus sp. EC116

AU - Kim, Min Soo

AU - Woo, Mi Hee

AU - Chang, Young Hyo

AU - Chung, Namhyun

AU - Kim, Joong Su

PY - 2016/4/1

Y1 - 2016/4/1

N2 - In our present study, a new Endo-1,4-β-xylanase (EC 3.2.1.8) was isolated, which belongs to glycosyl hydrolase family 10 member. The new enzyme designated as xynA was expressed for biochemical characterization. The xynA xylanase was identified in Paenibacillus sp. EC116. The novel gene had the size of 2673 base pairs, which correspond to 891 amino acid residues. The expressed enzyme has a size of ~100 kDa. The amino acid sequence was similar to that of endo-1,4-beta-xylanase from Paenibacillus sp. FSL R5-192 (ETT36211.1) (96 % identical). The xylanase has an optimal temperature of 40 °C and the pH optimum of 6.0. The specific activity of the xylanase toward birchwood xylan was about 0.69 μmol min−1 mg−1, the Vmax value of 1.639 μmol mg−1 min−1, and the Km value of 35.1 mg ml−1. The EC116 xylanase was relatively stable up to 60 °C. Xylanase enzymes have numerous industrial applications, which need to meet the specific requirements for each application. We hope that our EC116 xylanase is one of the candidates for commercial applications.

AB - In our present study, a new Endo-1,4-β-xylanase (EC 3.2.1.8) was isolated, which belongs to glycosyl hydrolase family 10 member. The new enzyme designated as xynA was expressed for biochemical characterization. The xynA xylanase was identified in Paenibacillus sp. EC116. The novel gene had the size of 2673 base pairs, which correspond to 891 amino acid residues. The expressed enzyme has a size of ~100 kDa. The amino acid sequence was similar to that of endo-1,4-beta-xylanase from Paenibacillus sp. FSL R5-192 (ETT36211.1) (96 % identical). The xylanase has an optimal temperature of 40 °C and the pH optimum of 6.0. The specific activity of the xylanase toward birchwood xylan was about 0.69 μmol min−1 mg−1, the Vmax value of 1.639 μmol mg−1 min−1, and the Km value of 35.1 mg ml−1. The EC116 xylanase was relatively stable up to 60 °C. Xylanase enzymes have numerous industrial applications, which need to meet the specific requirements for each application. We hope that our EC116 xylanase is one of the candidates for commercial applications.

KW - Glycosyl hydrolase family 10

KW - Paenibacillus sp

KW - Saccharification

KW - Xylanase

KW - Β-glucosidase

UR - http://www.scopus.com/inward/record.url?scp=84977553933&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84977553933&partnerID=8YFLogxK

U2 - 10.1007/s13765-016-0159-6

DO - 10.1007/s13765-016-0159-6

M3 - Article

AN - SCOPUS:84977553933

VL - 59

SP - 313

EP - 320

JO - Applied Biological Chemistry

JF - Applied Biological Chemistry

SN - 2468-0834

IS - 2

ER -