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Novel GH115 xylan α-1,2-glucuronidases with distinct preferences for xylan-derived oligomers and polymers

Leontakianakou, Savvina LU ; Le, Simone Baltzer ; Sundin, Anders LU ; Jasilionis, Andrius LU ; Nguyen, Giung-Son ; Nordborg, Anna ; Gottumukkala, Lalitha D. ; Grey, Carl LU orcid ; Lewin, Anna Sofia and Nordberg Karlsson, Eva LU orcid (2026) In Protein Science 35(5).
Abstract
Natural polymers are promising sustainable materials for diverse applications. Xylans, major components of hemicellulose, exhibit origin-dependent substitution patterns that determine their physicochemical properties. Targeted enzymatic modification of these substituents offers a mild and precise approach for tailoring the polymer's characteristics. Glucuronidases (EC 3.2.1.139) and xylan α-1,2-glucuronosidases (EC 3.2.1.131) are carbohydrate active enzymes that specifically remove the common glucuronic acid and 4-O-methyl d-glucuronic acid side branches of xylans/xylooligosaccharides from different hardwood and softwood sources. These enzymes are, dependent on sequence and structure, occurring in three glycoside hydrolase families (GH4,... (More)
Natural polymers are promising sustainable materials for diverse applications. Xylans, major components of hemicellulose, exhibit origin-dependent substitution patterns that determine their physicochemical properties. Targeted enzymatic modification of these substituents offers a mild and precise approach for tailoring the polymer's characteristics. Glucuronidases (EC 3.2.1.139) and xylan α-1,2-glucuronosidases (EC 3.2.1.131) are carbohydrate active enzymes that specifically remove the common glucuronic acid and 4-O-methyl d-glucuronic acid side branches of xylans/xylooligosaccharides from different hardwood and softwood sources. These enzymes are, dependent on sequence and structure, occurring in three glycoside hydrolase families (GH4, GH67 and GH115). GH115 predominantly includes xylan α-1,2-glucuronosidases, but the number of characterized enzymes is low. In this study, 22 novel GH115 candidates were identified through a combination of automated and manual sequence mining from databases, for evaluation of their production, function and storage possibilities. Twenty enzymes were produced in active form in crude extracts, while only four remained soluble for extended time periods post purification. These four GH115 candidates include first time reported monomeric enzymes, and while all were active on polymeric xylan, their specific activity and activity-ratio on polysaccharides/oligosaccharides of beechwood xylan differed significantly. Structural models created by AlphaFold3, and different length oligosaccharides were docked in the catalytic clefts. The presence of an additional domain, and the position of a mobile loop affected oligomerization and activity on polymeric substrates, respectively, resulting in differences in specific activity and preference for polymeric substrates. (Less)
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author
; ; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Protein Science
volume
35
issue
5
article number
e70571
pages
22 pages
publisher
The Protein Society
ISSN
1469-896X
DOI
10.1002/pro.70571
language
English
LU publication?
yes
id
ad8045a9-fb9e-413c-b559-4d977b96c995
date added to LUP
2026-04-09 18:43:40
date last changed
2026-04-13 13:01:22
@article{ad8045a9-fb9e-413c-b559-4d977b96c995,
  abstract     = {{Natural polymers are promising sustainable materials for diverse applications. Xylans, major components of hemicellulose, exhibit origin-dependent substitution patterns that determine their physicochemical properties. Targeted enzymatic modification of these substituents offers a mild and precise approach for tailoring the polymer's characteristics. Glucuronidases (EC 3.2.1.139) and xylan α-1,2-glucuronosidases (EC 3.2.1.131) are carbohydrate active enzymes that specifically remove the common glucuronic acid and 4-O-methyl d-glucuronic acid side branches of xylans/xylooligosaccharides from different hardwood and softwood sources. These enzymes are, dependent on sequence and structure, occurring in three glycoside hydrolase families (GH4, GH67 and GH115). GH115 predominantly includes xylan α-1,2-glucuronosidases, but the number of characterized enzymes is low. In this study, 22 novel GH115 candidates were identified through a combination of automated and manual sequence mining from databases, for evaluation of their production, function and storage possibilities. Twenty enzymes were produced in active form in crude extracts, while only four remained soluble for extended time periods post purification. These four GH115 candidates include first time reported monomeric enzymes, and while all were active on polymeric xylan, their specific activity and activity-ratio on polysaccharides/oligosaccharides of beechwood xylan differed significantly. Structural models created by AlphaFold3, and different length oligosaccharides were docked in the catalytic clefts. The presence of an additional domain, and the position of a mobile loop affected oligomerization and activity on polymeric substrates, respectively, resulting in differences in specific activity and preference for polymeric substrates.}},
  author       = {{Leontakianakou, Savvina and Le, Simone Baltzer and Sundin, Anders and Jasilionis, Andrius and Nguyen, Giung-Son and Nordborg, Anna and Gottumukkala, Lalitha D. and Grey, Carl and Lewin, Anna Sofia and Nordberg Karlsson, Eva}},
  issn         = {{1469-896X}},
  language     = {{eng}},
  month        = {{04}},
  number       = {{5}},
  publisher    = {{The Protein Society}},
  series       = {{Protein Science}},
  title        = {{Novel GH115 xylan α-1,2-glucuronidases with distinct preferences for xylan-derived oligomers and polymers}},
  url          = {{http://dx.doi.org/10.1002/pro.70571}},
  doi          = {{10.1002/pro.70571}},
  volume       = {{35}},
  year         = {{2026}},
}