Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans

Haisheng Wang; Wenqin He; Peixia Jiang; Yanlei Yu; Lei Lin; Xiaojun Sun; Mattheos Koffas; Fuming Zhang; Robert J. Linhardt

doi:10.1007/s10719-017-9786-3

Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans

Haisheng Wang, Wenqin He, Peixia Jiang, Yanlei Yu, Lei Lin, Xiaojun Sun, Mattheos Koffas, Fuming Zhang, Robert J. Linhardt

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

9 Scopus citations

Abstract

There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.

Original language	English
Pages (from-to)	643-649
Number of pages	7
Journal	Glycoconjugate Journal
Volume	34
Issue number	5
DOIs	https://doi.org/10.1007/s10719-017-9786-3
State	Published - 1 Oct 2017
Externally published	Yes

Keywords

Hydrolase
Keratan sulfate, glycosaminoglycan
Keratanase II
Mass spectrometry
Protein engineering

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10.1007/s10719-017-9786-3

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title = "Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans",

abstract = "There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.",

keywords = "Hydrolase, Keratan sulfate, glycosaminoglycan, Keratanase II, Mass spectrometry, Protein engineering",

author = "Haisheng Wang and Wenqin He and Peixia Jiang and Yanlei Yu and Lei Lin and Xiaojun Sun and Mattheos Koffas and Fuming Zhang and Linhardt, {Robert J.}",

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T1 - Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans

AU - Wang, Haisheng

AU - He, Wenqin

AU - Jiang, Peixia

AU - Yu, Yanlei

AU - Lin, Lei

AU - Sun, Xiaojun

AU - Koffas, Mattheos

AU - Zhang, Fuming

AU - Linhardt, Robert J.

PY - 2017/10/1

Y1 - 2017/10/1

N2 - There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.

AB - There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.

KW - Hydrolase

KW - Keratan sulfate, glycosaminoglycan

KW - Keratanase II

KW - Mass spectrometry

KW - Protein engineering

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DO - 10.1007/s10719-017-9786-3

M3 - Article

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SN - 0282-0080

VL - 34

SP - 643

EP - 649

JO - Glycoconjugate Journal

JF - Glycoconjugate Journal

IS - 5

ER -

Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans

Abstract

Keywords

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