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Novel Function of CtXyn5A from Acetivibrio thermocellus: Dual Arabinoxylanase and Feruloyl Esterase Activity Occur in the Same Active Site

Schmitz, Eva LU ; Leontakianakou, Savvina LU ; Adlercreutz, Patrick LU orcid ; Nordberg Karlsson, Eva LU orcid and Linares-Pastén, Javier A. LU orcid (2022)
Abstract
Uncharacterized side activities of enzymes can have significant negative effects on reaction products and yields. Hence, their identification and characterization is crucial for the development of successful reaction systems. Here, we report the presence of feruloyl esterase activity in CtXyn5A from Acetivibrio thermocellus besides its well-known arabinoxylanase activity for the first time. Both reaction types appear to be catalysed in the same active site in two subsequential steps. The ferulic acid substituent is cleaved off first, followed by the hydrolysis of the xylan backbone. The esterase activity on complex carbohydrates was found to be higher than the one of a designated ferulic acid esterase (E-FAERU). Therefore, we... (More)
Uncharacterized side activities of enzymes can have significant negative effects on reaction products and yields. Hence, their identification and characterization is crucial for the development of successful reaction systems. Here, we report the presence of feruloyl esterase activity in CtXyn5A from Acetivibrio thermocellus besides its well-known arabinoxylanase activity for the first time. Both reaction types appear to be catalysed in the same active site in two subsequential steps. The ferulic acid substituent is cleaved off first, followed by the hydrolysis of the xylan backbone. The esterase activity on complex carbohydrates was found to be higher than the one of a designated ferulic acid esterase (E-FAERU). Therefore, we conclude that the enzyme exhibits a dual function rather than an esterase side activity. (Less)
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author
; ; ; and
organization
publishing date
type
Working paper/Preprint
publication status
published
subject
keywords
Enzyme catalysis, Multifunctional enzymes, Arabino-xylanase, Feruloyl esterase, Carbohydrates
pages
7 pages
publisher
ChemRxiv
DOI
10.26434/chemrxiv-2022-dt3bb
language
English
LU publication?
yes
id
3b6ce123-c70b-43f1-a3eb-3178ef74b2fe
date added to LUP
2022-06-28 21:04:01
date last changed
2022-07-25 12:16:36
@misc{3b6ce123-c70b-43f1-a3eb-3178ef74b2fe,
  abstract     = {{Uncharacterized side activities of enzymes can have significant negative effects on reaction products and yields. Hence, their identification and characterization is crucial for the development of successful reaction systems. Here, we report the presence of feruloyl esterase activity in <i>Ct</i>Xyn5A from <i>Acetivibrio thermocellus</i> besides its well-known arabinoxylanase activity for the first time. Both reaction types appear to be catalysed in the same active site in two subsequential steps. The ferulic acid substituent is cleaved off first, followed by the hydrolysis of the xylan backbone. The esterase activity on complex carbohydrates was found to be higher than the one of a designated ferulic acid esterase (E-FAERU). Therefore, we conclude that the enzyme exhibits a dual function rather than an esterase side activity.}},
  author       = {{Schmitz, Eva and Leontakianakou, Savvina and Adlercreutz, Patrick and Nordberg Karlsson, Eva and Linares-Pastén, Javier A.}},
  keywords     = {{Enzyme catalysis; Multifunctional enzymes; Arabino-xylanase; Feruloyl esterase; Carbohydrates}},
  language     = {{eng}},
  month        = {{05}},
  note         = {{Preprint}},
  publisher    = {{ChemRxiv}},
  title        = {{Novel Function of <i>Ct</i>Xyn5A from <i>Acetivibrio thermocellus</i>: Dual Arabinoxylanase and Feruloyl Esterase Activity Occur in the Same Active Site}},
  url          = {{http://dx.doi.org/10.26434/chemrxiv-2022-dt3bb}},
  doi          = {{10.26434/chemrxiv-2022-dt3bb}},
  year         = {{2022}},
}