Structure, function, and protein engineering of GH53 β-1,4-galactanases
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Structure, function, and protein engineering of GH53 β-1,4-galactanases. / Muderspach, Sebastian J.; Jensen, Kenneth; Krogh, Kristian B.R.M.; Lo Leggio, Leila.
Glycoside Hydrolases: Biochemistry, Biophysics, and Biotechnology. Elsevier, 2023. s. 295-322.Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt
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TY - CHAP
T1 - Structure, function, and protein engineering of GH53 β-1,4-galactanases
AU - Muderspach, Sebastian J.
AU - Jensen, Kenneth
AU - Krogh, Kristian B.R.M.
AU - Lo Leggio, Leila
N1 - Publisher Copyright: © 2023 Elsevier Inc. All rights reserved.
PY - 2023
Y1 - 2023
N2 - In this review, we introduce the activities of endo-β-1,4-galactanases and related enzymes, their biological niches, and biological function. Endo-β-1,4-galactanases are classified in the glycoside hydrolase family 53 in the CAZy database (GH53) and degrade β-1,4-linked galactans and arabinogalactans. These substrates are found as sidechains decorating the backbone of rhamnogalacturonan type I, a “hairy” part of pectin. Pectin is found in the primary cell walls of nonwoody plants and enzymatic degradation of the pectin network is of interest in the production of, e.g., biofuel, fruit juice, and animal feed. β-1,4-Galactanases have also drawn interest due to their importance in the production and metabolism of prebiotic galactooligosaccharides used in formula milk. To date, several structures of endo-β-1,4-galactanases originating from a variety of organisms are known, which highlight structural variance in the length of substrate-binding sites. Based on these structures, we provide here a comprehensive overview on the structure-function relationship within the GH53 family. The acquired structural knowledge has led to engineering of β-1,4-galactanases to alter their biophysical and biochemical features and increase their applicability in industry.
AB - In this review, we introduce the activities of endo-β-1,4-galactanases and related enzymes, their biological niches, and biological function. Endo-β-1,4-galactanases are classified in the glycoside hydrolase family 53 in the CAZy database (GH53) and degrade β-1,4-linked galactans and arabinogalactans. These substrates are found as sidechains decorating the backbone of rhamnogalacturonan type I, a “hairy” part of pectin. Pectin is found in the primary cell walls of nonwoody plants and enzymatic degradation of the pectin network is of interest in the production of, e.g., biofuel, fruit juice, and animal feed. β-1,4-Galactanases have also drawn interest due to their importance in the production and metabolism of prebiotic galactooligosaccharides used in formula milk. To date, several structures of endo-β-1,4-galactanases originating from a variety of organisms are known, which highlight structural variance in the length of substrate-binding sites. Based on these structures, we provide here a comprehensive overview on the structure-function relationship within the GH53 family. The acquired structural knowledge has led to engineering of β-1,4-galactanases to alter their biophysical and biochemical features and increase their applicability in industry.
KW - Biomass
KW - Galactooligosaccharides (GOS)
KW - Glycoside hydrolase
KW - Pectin
KW - Structural studies
U2 - 10.1016/B978-0-323-91805-3.00018-6
DO - 10.1016/B978-0-323-91805-3.00018-6
M3 - Book chapter
AN - SCOPUS:85161132677
SN - 9780323972086
SP - 295
EP - 322
BT - Glycoside Hydrolases
PB - Elsevier
ER -
ID: 374458419