Production of xylanase from a novel engineered Pichia pastoris and application to enzymatic hydrolysis process for biorefinery

Chan Kyum Kim; Han Suk Choi; Sang Jun Lee; Ja Hyun Lee; Ju Hun Lee; Hah Young Yoo; Sung Ok Han; Seung Wook Kim

doi:10.1016/j.procbio.2017.11.001

Production of xylanase from a novel engineered Pichia pastoris and application to enzymatic hydrolysis process for biorefinery

Chan Kyum Kim, Han Suk Choi, Sang Jun Lee, Ja Hyun Lee, Ju Hun Lee, Hah Young Yoo, Sung Ok Han, Seung Wook Kim

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

20 Citations (Scopus)

Abstract

In this study, the xylanase gene from Cellulomonas flavigena KCTC 9104 was cloned into pPICZαB and expressed in Pichia pastoris X-33. An extracellular endo-1,4-β-xylanase was produced by novel engineered P. pastoris (rXynCf) and purified by Ni-NTA affinity column. Characterization of rXynCf was performed and results are as follows: 38 kDa molecular weight, 55 °C optimum temperature and optimum pH of 6. Under the conditions, the K_m and V_max of rXynCf were 3.6 ± 0.08 mg/mL and 4505 ± 52 μmol/min mg, respectively. rXynCf was applied in enzymatic hydrolysis process for sugars production from lignocellulosic biomass. Empty fruit bunch (EFB) was selected as a feedstock, and the total sugars conversion was found to be 3.8%, meanwhile the conversion by alkaline pretreatment improved approximately 16-fold (61.1%). In addition, rXynCf shows similar xylose conversion to commercial xylanase. Therefore, due to its properties, rXynCf has considerable potential in biorefinery applications.

Original language	English
Pages (from-to)	130-135
Number of pages	6
Journal	Process Biochemistry
Volume	65
DOIs	https://doi.org/10.1016/j.procbio.2017.11.001
Publication status	Published - 2018 Feb

Bibliographical note

Publisher Copyright:
© 2017 Elsevier Ltd

Keywords

Biorefinery
Cellulomonas flavigena
Enzymatic hydrolysis
Pichia pastoris
Xylanase

ASJC Scopus subject areas

Bioengineering
Biochemistry
Applied Microbiology and Biotechnology

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10.1016/j.procbio.2017.11.001

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title = "Production of xylanase from a novel engineered Pichia pastoris and application to enzymatic hydrolysis process for biorefinery",

abstract = "In this study, the xylanase gene from Cellulomonas flavigena KCTC 9104 was cloned into pPICZαB and expressed in Pichia pastoris X-33. An extracellular endo-1,4-β-xylanase was produced by novel engineered P. pastoris (rXynCf) and purified by Ni-NTA affinity column. Characterization of rXynCf was performed and results are as follows: 38 kDa molecular weight, 55 °C optimum temperature and optimum pH of 6. Under the conditions, the Km and Vmax of rXynCf were 3.6 ± 0.08 mg/mL and 4505 ± 52 μmol/min mg, respectively. rXynCf was applied in enzymatic hydrolysis process for sugars production from lignocellulosic biomass. Empty fruit bunch (EFB) was selected as a feedstock, and the total sugars conversion was found to be 3.8%, meanwhile the conversion by alkaline pretreatment improved approximately 16-fold (61.1%). In addition, rXynCf shows similar xylose conversion to commercial xylanase. Therefore, due to its properties, rXynCf has considerable potential in biorefinery applications.",

keywords = "Biorefinery, Cellulomonas flavigena, Enzymatic hydrolysis, Pichia pastoris, Xylanase",

author = "Kim, {Chan Kyum} and Choi, {Han Suk} and Lee, {Sang Jun} and Lee, {Ja Hyun} and Lee, {Ju Hun} and Yoo, {Hah Young} and Han, {Sung Ok} and Kim, {Seung Wook}",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

year = "2018",

month = feb,

doi = "10.1016/j.procbio.2017.11.001",

language = "English",

volume = "65",

pages = "130--135",

journal = "Process Biochemistry",

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T1 - Production of xylanase from a novel engineered Pichia pastoris and application to enzymatic hydrolysis process for biorefinery

AU - Kim, Chan Kyum

AU - Choi, Han Suk

AU - Lee, Sang Jun

AU - Lee, Ja Hyun

AU - Lee, Ju Hun

AU - Yoo, Hah Young

AU - Han, Sung Ok

AU - Kim, Seung Wook

PY - 2018/2

Y1 - 2018/2

N2 - In this study, the xylanase gene from Cellulomonas flavigena KCTC 9104 was cloned into pPICZαB and expressed in Pichia pastoris X-33. An extracellular endo-1,4-β-xylanase was produced by novel engineered P. pastoris (rXynCf) and purified by Ni-NTA affinity column. Characterization of rXynCf was performed and results are as follows: 38 kDa molecular weight, 55 °C optimum temperature and optimum pH of 6. Under the conditions, the Km and Vmax of rXynCf were 3.6 ± 0.08 mg/mL and 4505 ± 52 μmol/min mg, respectively. rXynCf was applied in enzymatic hydrolysis process for sugars production from lignocellulosic biomass. Empty fruit bunch (EFB) was selected as a feedstock, and the total sugars conversion was found to be 3.8%, meanwhile the conversion by alkaline pretreatment improved approximately 16-fold (61.1%). In addition, rXynCf shows similar xylose conversion to commercial xylanase. Therefore, due to its properties, rXynCf has considerable potential in biorefinery applications.

AB - In this study, the xylanase gene from Cellulomonas flavigena KCTC 9104 was cloned into pPICZαB and expressed in Pichia pastoris X-33. An extracellular endo-1,4-β-xylanase was produced by novel engineered P. pastoris (rXynCf) and purified by Ni-NTA affinity column. Characterization of rXynCf was performed and results are as follows: 38 kDa molecular weight, 55 °C optimum temperature and optimum pH of 6. Under the conditions, the Km and Vmax of rXynCf were 3.6 ± 0.08 mg/mL and 4505 ± 52 μmol/min mg, respectively. rXynCf was applied in enzymatic hydrolysis process for sugars production from lignocellulosic biomass. Empty fruit bunch (EFB) was selected as a feedstock, and the total sugars conversion was found to be 3.8%, meanwhile the conversion by alkaline pretreatment improved approximately 16-fold (61.1%). In addition, rXynCf shows similar xylose conversion to commercial xylanase. Therefore, due to its properties, rXynCf has considerable potential in biorefinery applications.

KW - Biorefinery

KW - Cellulomonas flavigena

KW - Enzymatic hydrolysis

KW - Pichia pastoris

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DO - 10.1016/j.procbio.2017.11.001

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Production of xylanase from a novel engineered Pichia pastoris and application to enzymatic hydrolysis process for biorefinery

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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