TY - JOUR
T1 - Deciphering heterogeneous enzymatic surface reactions on xylan using surface plasmon resonance spectroscopy
AU - Schaubeder, Jana B.
AU - Fürk, Peter
AU - Amering, Richard
AU - Gsöls, Lena
AU - Ravn, Jonas
AU - Nypelö, Tiina
AU - Spirk, Stefan
N1 - Publisher Copyright:
© 2024 The Author(s)
PY - 2024/8/1
Y1 - 2024/8/1
N2 - Xylans' unique properties make it attractive for a variety of industries, including paper, food, and biochemical production. While for some applications the preservation of its natural structure is crucial, for others the degradation into monosaccharides is essential. For the complete breakdown, the use of several enzymes is required, due to its structural complexity. In fact, the specificity of enzymatically-catalyzed reactions is guided by the surface, limiting or regulating accessibility and serving structurally encoded input guiding the actions of the enzymes. Here, we investigate enzymes at surfaces rich in xylan using surface plasmon resonance spectroscopy. The influence of diffusion and changes in substrate morphology is studied via enzyme surface kinetics simulations, yielding reaction rates and constants. We propose kinetic models, which can be applied to the degradation of multilayer biopolymer films. The most advanced model was verified by its successful application to the degradation of a thin film of polyhydroxybutyrate treated with a polyhydroxybutyrate-depolymerase. The herein derived models can be employed to quantify the degradation kinetics of various enzymes on biopolymers in heterogeneous environments, often prevalent in industrial processes. The identification of key factors influencing reaction rates such as inhibition will contribute to the quantification of intricate dynamics in complex systems.
AB - Xylans' unique properties make it attractive for a variety of industries, including paper, food, and biochemical production. While for some applications the preservation of its natural structure is crucial, for others the degradation into monosaccharides is essential. For the complete breakdown, the use of several enzymes is required, due to its structural complexity. In fact, the specificity of enzymatically-catalyzed reactions is guided by the surface, limiting or regulating accessibility and serving structurally encoded input guiding the actions of the enzymes. Here, we investigate enzymes at surfaces rich in xylan using surface plasmon resonance spectroscopy. The influence of diffusion and changes in substrate morphology is studied via enzyme surface kinetics simulations, yielding reaction rates and constants. We propose kinetic models, which can be applied to the degradation of multilayer biopolymer films. The most advanced model was verified by its successful application to the degradation of a thin film of polyhydroxybutyrate treated with a polyhydroxybutyrate-depolymerase. The herein derived models can be employed to quantify the degradation kinetics of various enzymes on biopolymers in heterogeneous environments, often prevalent in industrial processes. The identification of key factors influencing reaction rates such as inhibition will contribute to the quantification of intricate dynamics in complex systems.
KW - Biopolymers
KW - Enzymatic degradation
KW - Multilayer thin films
KW - Polyhydroxybutyrate
KW - Reaction kinetics
KW - Xylanases
UR - http://www.scopus.com/inward/record.url?scp=85190401165&partnerID=8YFLogxK
U2 - 10.1016/j.carbpol.2024.122137
DO - 10.1016/j.carbpol.2024.122137
M3 - Article
AN - SCOPUS:85190401165
SN - 0144-8617
VL - 337
JO - Carbohydrate Polymers
JF - Carbohydrate Polymers
M1 - 122137
ER -