Xylan-cellulose thin film platform for assessing xylanase activity

Jana B. Schaubeder; Jonas L. Ravn; Eliott J. Q. Orzan; Joao H. C. Manfrao-Netto; Cecilia Geijer; Tiina Nypelö; Stefan Spirk

doi:10.1016/j.carbpol.2022.119737

Xylan-cellulose thin film platform for assessing xylanase activity

Jana B. Schaubeder
, Jonas L. Ravn
, Eliott J. Q. Orzan
, Joao H. C. Manfrao-Netto
, Cecilia Geijer
, Tiina Nypelö
, Stefan Spirk

Not published at Aalto University

Graz University of Technology
Chalmers University of Technology
Wallenberg Wood Science Center

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

17 Citations (Scopus)

Abstract

Enzymatic degradation of plant polysaccharide networks is a complex process that involves disrupting an intimate assembly of cellulose and hemicelluloses in fibrous matrices. To mimic this assembly and to elucidate the efficiency of enzymatic degradation in a rapid way, models with physicochemical equivalence to natural systems are needed. Here, we employ xylan-coated cellulose thin films to monitor the hydrolyzing activity of an endo-1,4-beta-xylanase. In situ surface plasmon resonance spectroscopy (SPRS) revealed a decrease in xylan areal mass ranging from 0.01± 0.02 to 0.52 ± 0.04 mg.m^-2. The extent of digestion correlates to increasing xylanase concentration. In addition, ex situ determination of released monosaccharides revealed that incubation time was also a significant factor in degradation (P > 0.01). For both experiments, atomic force microscopy confirmed the removal of xylans from the cellulose thin films. We provide a new model platform that offers nanoscale sensitivity for investigating biopolymer interactions and their susceptibility to enzymatic hydrolysis.

Original language	English
Article number	119737
Number of pages	9
Journal	Carbohydrate Polymers
Volume	294
DOIs	https://doi.org/10.1016/j.carbpol.2022.119737
Publication status	Published - 15 Oct 2022
MoE publication type	A1 Journal article-refereed

Funding

This work has received funding from the European Union's Horizon 2020-Research and Innovation Framework Programme under grant agreement No 964430. TN acknowledges the funding from Wallenberg Wood Science Center and Area of Advance Materials, Chalmers University of Technology.

Keywords

Xylan
Xylanase
Trimethylsilyl cellulose
Thin films
Biopolymer
WATER INTERACTIONS
ULTRATHIN FILMS
ADSORPTION
SURFACE
XYLOGLUCAN
FIBER
WOOD
HEMICELLULOSES
ARCHITECTURE
BIOPOLYMERS

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10.1016/j.carbpol.2022.119737

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@article{a75e423f7f2d4cb1a7d1202bb59ea190,

title = "Xylan-cellulose thin film platform for assessing xylanase activity",

abstract = "Enzymatic degradation of plant polysaccharide networks is a complex process that involves disrupting an intimate assembly of cellulose and hemicelluloses in fibrous matrices. To mimic this assembly and to elucidate the efficiency of enzymatic degradation in a rapid way, models with physicochemical equivalence to natural systems are needed. Here, we employ xylan-coated cellulose thin films to monitor the hydrolyzing activity of an endo-1,4-beta-xylanase. In situ surface plasmon resonance spectroscopy (SPRS) revealed a decrease in xylan areal mass ranging from 0.01± 0.02 to 0.52 ± 0.04 mg.m-2. The extent of digestion correlates to increasing xylanase concentration. In addition, ex situ determination of released monosaccharides revealed that incubation time was also a significant factor in degradation (P > 0.01). For both experiments, atomic force microscopy confirmed the removal of xylans from the cellulose thin films. We provide a new model platform that offers nanoscale sensitivity for investigating biopolymer interactions and their susceptibility to enzymatic hydrolysis.",

keywords = "Xylan, Xylanase, Trimethylsilyl cellulose, Thin films, Biopolymer, WATER INTERACTIONS, ULTRATHIN FILMS, ADSORPTION, SURFACE, XYLOGLUCAN, FIBER, WOOD, HEMICELLULOSES, ARCHITECTURE, BIOPOLYMERS",

author = "Schaubeder, \{Jana B.\} and Ravn, \{Jonas L.\} and Orzan, \{Eliott J. Q.\} and Manfrao-Netto, \{Joao H. C.\} and Cecilia Geijer and Tiina Nypel{\"o} and Stefan Spirk",

year = "2022",

month = oct,

day = "15",

doi = "10.1016/j.carbpol.2022.119737",

language = "English",

volume = "294",

journal = "Carbohydrate Polymers",

issn = "0144-8617",

publisher = "Elsevier",

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TY - JOUR

T1 - Xylan-cellulose thin film platform for assessing xylanase activity

AU - Schaubeder, Jana B.

AU - Ravn, Jonas L.

AU - Orzan, Eliott J. Q.

AU - Manfrao-Netto, Joao H. C.

AU - Geijer, Cecilia

AU - Nypelö, Tiina

AU - Spirk, Stefan

PY - 2022/10/15

Y1 - 2022/10/15

N2 - Enzymatic degradation of plant polysaccharide networks is a complex process that involves disrupting an intimate assembly of cellulose and hemicelluloses in fibrous matrices. To mimic this assembly and to elucidate the efficiency of enzymatic degradation in a rapid way, models with physicochemical equivalence to natural systems are needed. Here, we employ xylan-coated cellulose thin films to monitor the hydrolyzing activity of an endo-1,4-beta-xylanase. In situ surface plasmon resonance spectroscopy (SPRS) revealed a decrease in xylan areal mass ranging from 0.01± 0.02 to 0.52 ± 0.04 mg.m-2. The extent of digestion correlates to increasing xylanase concentration. In addition, ex situ determination of released monosaccharides revealed that incubation time was also a significant factor in degradation (P > 0.01). For both experiments, atomic force microscopy confirmed the removal of xylans from the cellulose thin films. We provide a new model platform that offers nanoscale sensitivity for investigating biopolymer interactions and their susceptibility to enzymatic hydrolysis.

AB - Enzymatic degradation of plant polysaccharide networks is a complex process that involves disrupting an intimate assembly of cellulose and hemicelluloses in fibrous matrices. To mimic this assembly and to elucidate the efficiency of enzymatic degradation in a rapid way, models with physicochemical equivalence to natural systems are needed. Here, we employ xylan-coated cellulose thin films to monitor the hydrolyzing activity of an endo-1,4-beta-xylanase. In situ surface plasmon resonance spectroscopy (SPRS) revealed a decrease in xylan areal mass ranging from 0.01± 0.02 to 0.52 ± 0.04 mg.m-2. The extent of digestion correlates to increasing xylanase concentration. In addition, ex situ determination of released monosaccharides revealed that incubation time was also a significant factor in degradation (P > 0.01). For both experiments, atomic force microscopy confirmed the removal of xylans from the cellulose thin films. We provide a new model platform that offers nanoscale sensitivity for investigating biopolymer interactions and their susceptibility to enzymatic hydrolysis.

KW - Xylan

KW - Xylanase

KW - Trimethylsilyl cellulose

KW - Thin films

KW - Biopolymer

KW - WATER INTERACTIONS

KW - ULTRATHIN FILMS

KW - ADSORPTION

KW - SURFACE

KW - XYLOGLUCAN

KW - FIBER

KW - WOOD

KW - HEMICELLULOSES

KW - ARCHITECTURE

KW - BIOPOLYMERS

UR - https://www.scopus.com/pages/publications/85133655502

U2 - 10.1016/j.carbpol.2022.119737

DO - 10.1016/j.carbpol.2022.119737

M3 - Article

SN - 0144-8617

VL - 294

JO - Carbohydrate Polymers

JF - Carbohydrate Polymers

M1 - 119737

ER -

Xylan-cellulose thin film platform for assessing xylanase activity

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Keywords

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