Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds

Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2)...
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Autor*in:	Feng Tang [verfasserIn] Daiwen Chen [verfasserIn] Bing Yu [verfasserIn] Yuheng Luo [verfasserIn] Ping Zheng [verfasserIn] Xiangbing Mao [verfasserIn] Jie Yu [verfasserIn] Jun He [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes

Übergeordnetes Werk:	In: Electronic Journal of Biotechnology - Elsevier, 2016, 26(2017), C, Seite 52-59
Übergeordnetes Werk:	volume:26 ; year:2017 ; number:C ; pages:52-59

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.ejbt.2017.01.001

Katalog-ID:	DOAJ034867244

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520			\|a Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein.
650		4	\|a Disulfide bond introduction
650		4	\|a Feed pelleting
650		4	\|a Glycoside hydrolase
650		4	\|a Industry applications
650		4	\|a Pulp bleaching
650		4	\|a Site-directed mutagenesis
650		4	\|a Stable xylanase
650		4	\|a Xylan degradation
650		4	\|a Xylanolytic enzymes
653		0	\|a Biotechnology
653		0	\|a Biology (General)
700	0		\|a Daiwen Chen \|e verfasserin \|4 aut
700	0		\|a Bing Yu \|e verfasserin \|4 aut
700	0		\|a Yuheng Luo \|e verfasserin \|4 aut
700	0		\|a Ping Zheng \|e verfasserin \|4 aut
700	0		\|a Xiangbing Mao \|e verfasserin \|4 aut
700	0		\|a Jie Yu \|e verfasserin \|4 aut
700	0		\|a Jun He \|e verfasserin \|4 aut
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allfields	10.1016/j.ejbt.2017.01.001 doi (DE-627)DOAJ034867244 (DE-599)DOAJ6d8172b839c24f7480fb32aae675fb0a DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Feng Tang verfasserin aut Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein. Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes Biotechnology Biology (General) Daiwen Chen verfasserin aut Bing Yu verfasserin aut Yuheng Luo verfasserin aut Ping Zheng verfasserin aut Xiangbing Mao verfasserin aut Jie Yu verfasserin aut Jun He verfasserin aut In Electronic Journal of Biotechnology Elsevier, 2016 26(2017), C, Seite 52-59 (DE-627)320604713 (DE-600)2020598-3 07173458 nnns volume:26 year:2017 number:C pages:52-59 https://doi.org/10.1016/j.ejbt.2017.01.001 kostenfrei https://doaj.org/article/6d8172b839c24f7480fb32aae675fb0a kostenfrei http://www.sciencedirect.com/science/article/pii/S0717345817300015 kostenfrei https://doaj.org/toc/0717-3458 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 26 2017 C 52-59
spelling	10.1016/j.ejbt.2017.01.001 doi (DE-627)DOAJ034867244 (DE-599)DOAJ6d8172b839c24f7480fb32aae675fb0a DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Feng Tang verfasserin aut Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein. Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes Biotechnology Biology (General) Daiwen Chen verfasserin aut Bing Yu verfasserin aut Yuheng Luo verfasserin aut Ping Zheng verfasserin aut Xiangbing Mao verfasserin aut Jie Yu verfasserin aut Jun He verfasserin aut In Electronic Journal of Biotechnology Elsevier, 2016 26(2017), C, Seite 52-59 (DE-627)320604713 (DE-600)2020598-3 07173458 nnns volume:26 year:2017 number:C pages:52-59 https://doi.org/10.1016/j.ejbt.2017.01.001 kostenfrei https://doaj.org/article/6d8172b839c24f7480fb32aae675fb0a kostenfrei http://www.sciencedirect.com/science/article/pii/S0717345817300015 kostenfrei https://doaj.org/toc/0717-3458 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 26 2017 C 52-59
allfields_unstemmed	10.1016/j.ejbt.2017.01.001 doi (DE-627)DOAJ034867244 (DE-599)DOAJ6d8172b839c24f7480fb32aae675fb0a DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Feng Tang verfasserin aut Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein. Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes Biotechnology Biology (General) Daiwen Chen verfasserin aut Bing Yu verfasserin aut Yuheng Luo verfasserin aut Ping Zheng verfasserin aut Xiangbing Mao verfasserin aut Jie Yu verfasserin aut Jun He verfasserin aut In Electronic Journal of Biotechnology Elsevier, 2016 26(2017), C, Seite 52-59 (DE-627)320604713 (DE-600)2020598-3 07173458 nnns volume:26 year:2017 number:C pages:52-59 https://doi.org/10.1016/j.ejbt.2017.01.001 kostenfrei https://doaj.org/article/6d8172b839c24f7480fb32aae675fb0a kostenfrei http://www.sciencedirect.com/science/article/pii/S0717345817300015 kostenfrei https://doaj.org/toc/0717-3458 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 26 2017 C 52-59
allfieldsGer	10.1016/j.ejbt.2017.01.001 doi (DE-627)DOAJ034867244 (DE-599)DOAJ6d8172b839c24f7480fb32aae675fb0a DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Feng Tang verfasserin aut Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein. Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes Biotechnology Biology (General) Daiwen Chen verfasserin aut Bing Yu verfasserin aut Yuheng Luo verfasserin aut Ping Zheng verfasserin aut Xiangbing Mao verfasserin aut Jie Yu verfasserin aut Jun He verfasserin aut In Electronic Journal of Biotechnology Elsevier, 2016 26(2017), C, Seite 52-59 (DE-627)320604713 (DE-600)2020598-3 07173458 nnns volume:26 year:2017 number:C pages:52-59 https://doi.org/10.1016/j.ejbt.2017.01.001 kostenfrei https://doaj.org/article/6d8172b839c24f7480fb32aae675fb0a kostenfrei http://www.sciencedirect.com/science/article/pii/S0717345817300015 kostenfrei https://doaj.org/toc/0717-3458 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 26 2017 C 52-59
allfieldsSound	10.1016/j.ejbt.2017.01.001 doi (DE-627)DOAJ034867244 (DE-599)DOAJ6d8172b839c24f7480fb32aae675fb0a DE-627 ger DE-627 rakwb eng TP248.13-248.65 QH301-705.5 Feng Tang verfasserin aut Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein. Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes Biotechnology Biology (General) Daiwen Chen verfasserin aut Bing Yu verfasserin aut Yuheng Luo verfasserin aut Ping Zheng verfasserin aut Xiangbing Mao verfasserin aut Jie Yu verfasserin aut Jun He verfasserin aut In Electronic Journal of Biotechnology Elsevier, 2016 26(2017), C, Seite 52-59 (DE-627)320604713 (DE-600)2020598-3 07173458 nnns volume:26 year:2017 number:C pages:52-59 https://doi.org/10.1016/j.ejbt.2017.01.001 kostenfrei https://doaj.org/article/6d8172b839c24f7480fb32aae675fb0a kostenfrei http://www.sciencedirect.com/science/article/pii/S0717345817300015 kostenfrei https://doaj.org/toc/0717-3458 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2108 GBV_ILN_2111 GBV_ILN_2119 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 26 2017 C 52-59
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authorswithroles_txt_mv	Feng Tang @@aut@@ Daiwen Chen @@aut@@ Bing Yu @@aut@@ Yuheng Luo @@aut@@ Ping Zheng @@aut@@ Xiangbing Mao @@aut@@ Jie Yu @@aut@@ Jun He @@aut@@
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callnumber-first	T - Technology
author	Feng Tang
spellingShingle	Feng Tang misc TP248.13-248.65 misc QH301-705.5 misc Disulfide bond introduction misc Feed pelleting misc Glycoside hydrolase misc Industry applications misc Pulp bleaching misc Site-directed mutagenesis misc Stable xylanase misc Xylan degradation misc Xylanolytic enzymes misc Biotechnology misc Biology (General) Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds
authorStr	Feng Tang
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topic_title	TP248.13-248.65 QH301-705.5 Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds Disulfide bond introduction Feed pelleting Glycoside hydrolase Industry applications Pulp bleaching Site-directed mutagenesis Stable xylanase Xylan degradation Xylanolytic enzymes
topic	misc TP248.13-248.65 misc QH301-705.5 misc Disulfide bond introduction misc Feed pelleting misc Glycoside hydrolase misc Industry applications misc Pulp bleaching misc Site-directed mutagenesis misc Stable xylanase misc Xylan degradation misc Xylanolytic enzymes misc Biotechnology misc Biology (General)
topic_unstemmed	misc TP248.13-248.65 misc QH301-705.5 misc Disulfide bond introduction misc Feed pelleting misc Glycoside hydrolase misc Industry applications misc Pulp bleaching misc Site-directed mutagenesis misc Stable xylanase misc Xylan degradation misc Xylanolytic enzymes misc Biotechnology misc Biology (General)
topic_browse	misc TP248.13-248.65 misc QH301-705.5 misc Disulfide bond introduction misc Feed pelleting misc Glycoside hydrolase misc Industry applications misc Pulp bleaching misc Site-directed mutagenesis misc Stable xylanase misc Xylan degradation misc Xylanolytic enzymes misc Biotechnology misc Biology (General)
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title	Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds
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title_full	Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds
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doi_str_mv	10.1016/j.ejbt.2017.01.001
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title_sort	improving the thermostability of trichoderma reesei xylanase 2 by introducing disulfide bonds
callnumber	TP248.13-248.65
title_auth	Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds
abstract	Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein.
abstractGer	Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein.
abstract_unstemmed	Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein.
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title_short	Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds
url	https://doi.org/10.1016/j.ejbt.2017.01.001 https://doaj.org/article/6d8172b839c24f7480fb32aae675fb0a http://www.sciencedirect.com/science/article/pii/S0717345817300015 https://doaj.org/toc/0717-3458
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author2	Daiwen Chen Bing Yu Yuheng Luo Ping Zheng Xiangbing Mao Jie Yu Jun He
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up_date	2024-07-04T00:55:24.959Z
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fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">DOAJ034867244</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230307192820.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230227s2017 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.ejbt.2017.01.001</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)DOAJ034867244</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)DOAJ6d8172b839c24f7480fb32aae675fb0a</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="050" ind1=" " ind2="0"><subfield code="a">TP248.13-248.65</subfield></datafield><datafield tag="050" ind1=" " ind2="0"><subfield code="a">QH301-705.5</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Feng Tang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2017</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the β-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the β-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C14–52 (disulfide bond between β-sheets B2 and B3) and Xyn2C59–149 (disulfide bond between β-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the β-sheet core is due to the stable structure of the entire protein.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Disulfide bond introduction</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Feed pelleting</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glycoside hydrolase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Industry applications</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Pulp bleaching</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Site-directed mutagenesis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Stable xylanase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Xylan degradation</subfield></datafield><datafield tag="650" 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Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds

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