Cellulose in plants and chitin in shells and fungi form one of Earth’s largest renewable carbon reservoirs. By uncovering an unsuspected enzyme principle that loosens these resistant materials for further attack by other proteins, Vincent Eijsink transformed our understanding of how nature deconstructs biomass — and reshaped the technological foundation for converting plant waste into fuels, chemicals and materials capable of replacing fossil-derived products at industrial scale.
For decades, scientists believed they largely understood how nature dismantled its most resilient biological materials. In plant cell walls and in shells and fungi alike, the prevailing explanation centred on hydrolytic enzymes — proteins that cut long carbohydrate chains by slicing them into smaller fragments — as the dominant drivers of degradation.
Yet important questions remained unanswered.
As early as the 1950s, researchers had speculated that additional players must be involved in degrading polysaccharides — long chains of sugar molecules that form the structural backbone of materials such as cellulose and chitin — that resist breakdown because of their crystalline structure. The so-called C1–Cx hypothesis suggested that something more than the known cutting enzymes was needed — but for decades, no one could show clearly what that “something” was.
In 2005, Vincent Eijsink and his team provided the first clear demonstration that certain proteins long dismissed as passive chitin-binding factors dramatically enhance the activity of hydrolytic chitinases during the degradation of chitin — a tough structural polymer found in fungal cell walls and in the shells of insects and crustaceans.. The mechanism was not yet understood, but the finding confirmed that a long-suspected missing component was real.
Determined to resolve the mystery, Eijsink and his colleagues continued the search. Five years later, in a landmark 2010 study, they revealed what these proteins actually were: powerful oxidative enzymes.
Rather than cutting accessible chains, these enzymes attack the tightly packed crystalline regions of cellulose and chitin, introducing oxidative breaks that loosen the structure itself — creating entry points that hydrolytic enzymes alone cannot generate.
These enzymes are now known as lytic polysaccharide monooxygenases (LPMOs).
Their discovery showed that efficient biomass degradation is not only a matter of classical cellulases and chitinases. It depends on coordinated oxidative and hydrolytic chemistry working in concert.
“That was the moment we understood that degradation is not only a matter of classical enzymes,” Eijsink says. “Nature uses cooperation — oxidative attack to open dense structures before hydrolysis completes the process. Once we saw that, everything looked different.”
From a missing factor to a mechanistic principle
Scientists already knew that multiple hydrolytic enzymes work together — so-called endo-enzymes that attack chains internally, and exo-enzymes that trim them from the ends. What had never been convincingly demonstrated was the biochemical identity and function of the additional factor long proposed to disrupt crystalline structure.
Eijsink’s work provided that demonstration.
LPMOs introduce oxidative cuts directly into tightly packed crystalline regions of cellulose and chitin. These oxidative “nicks” weaken structural integrity, making the material accessible to hydrolytic enzymes and dramatically increasing overall degradation efficiency.
The implications extended far beyond enzymology.
Modern commercial enzyme formulations for biomass processing now routinely include lytic polysaccharide monooxygenases (LPMOs). These enzymes increase sugar yields from agricultural residues and woody biomass while reducing the total amount of enzyme needed — improving process economics and bringing bio-based fuels and materials closer to industrial competitiveness.
Professor Detlef Weigel, Chair of the Novonesis Biotechnology Prize Committee, explains:
“Vincent Eijsink resolved a long-standing paradox in polysaccharide enzymology,” says Professor Detlef Weigel. “By showing that oxidative chemistry is a core biological principle in the degradation of the planet’s most abundant polysaccharides, he fundamentally changed how the field understands biomass conversion — and how industry implements it.”
Making oxidative chemistry controllable
The initial breakthrough raised a new question: how exactly do these enzymes work?
Eijsink’s group moved from discovery to detailed mechanistic analysis of LPMOs at the molecular and atomistic level. Among other advances, they demonstrated that hydrogen peroxide can act as the immediate co-substrate in LPMO catalysis, refining our understanding of how oxidative breakdown actually works at the molecular level.
This insight clarified both the extraordinary efficiency of the enzymes and their sensitivity under uncontrolled conditions.
Understanding this chemistry proved essential for industrial scale-up. Oxidative power must be precisely controlled: too little limits efficiency; too much inactivates the enzyme.
“These enzymes are extraordinarily powerful,” Eijsink says. “But power without control destroys the system. Once we understood that hydrogen peroxide drives the reaction — and how quickly things go wrong when it is not regulated — we could begin to make the chemistry predictable and usable.”
From laboratory insight to industrial transformation
What began as a mechanistic puzzle in enzymology evolved into a foundational principle of the emerging bioeconomy.
Efficient breakdown of lignocellulosic biomass — plant material made up of tightly bound cellulose, hemicellulose and lignin — remains one of the central bottlenecks in second-generation biofuels, renewable chemicals and bio-based materials. By introducing oxidative cleavages directly into crystalline biomass, LPMOs increase saccharification yields, reduce total enzyme load and improve overall process economics — critical steps toward making bio-based production technologically and commercially viable.
Eijsink’s work has also influenced adjacent domains, including chitin valorisation, fibre modification and surface engineering of biomaterials. More recently, principles derived from oxidative enzyme systems are informing strategies for tackling other recalcitrant materials — including synthetic polymers such as plastics — extending the relevance of the discovery beyond natural biomass.
“Nature has evolved sophisticated solutions for modifying solid surfaces,” Eijsink explains. “If we understand those principles, we can adapt them to the sustainability challenges of our time.”
Shaping a new scientific discipline
The unique catalytic features of LPMOs have drawn attention well beyond enzymology. Insights from LPMO research have since inspired chemists to develop nature-inspired synthetic catalysts designed to improve efficiency and selectivity in greener chemical processes.
Beyond the mechanistic discoveries themselves, Eijsink has played a central role in building the international research community focused on oxidative enzymes acting on polysaccharides. What began as an unexpected observation has developed into a coherent and globally recognised research field.
He has supervised and mentored a generation of researchers who now lead independent programmes in enzymology and biotechnology across Europe and beyond. And now Vincent Eijsink receives the Novonesis Biotechnology Prize as a recognition of his valuable contributions to research and innovation within biotechnology.
“The work on LPMOs was transformative,” the Prize Committee states, “but equally important has been Vincent Eijsink’s sustained leadership in developing the field. He combined mechanistic depth with translational awareness, ensuring that fundamental science could inform industrial innovation.”
A new foundation for sustainable biotechnology
These discoveries did more than reshape a scientific field alone. They also exemplify the kind of fundamental insight with direct societal impact that the Novonesis Biotechnology Prize was established to recognise.
At its core, Vincent Eijsink’s work made it possible to extract more value from renewable biological materials while using less energy and fewer resources. By revealing how oxidative enzymes help unlock some of the planet’s most resistant natural structures, his research paved the way for more efficient, lower-emission conversion of plant waste into fuels, chemicals and materials at industrial scale.
“It started with curiosity about proteins that did not seem to do very much,” Eijsink reflects. “Step by step, we learned what they actually do. And once that became clear, the implications followed.”
Professor Detlef Weigel adds:
“This is work that reshaped an entire scientific field and translated directly into industrial impact,” Weigel says. “That combination is rare — and it defines truly transformative science.”
In connection with the official award ceremony on 24 April 2026, a public open lecture will be delivered by Vincent Eijsink. The lecture will take place at Technical University of Denmark on Thursday, 23 April, from 15:30 to 18:30. More information and registration at www.conferencemanager.dk/thenovonesisprizelecture.
About Vincent Eijsink
1986 MSc in Molecular Sciences (Biochemistry), Wageningen University, The Netherlands
1991 PhD in Biomolecular Sciences and Biotechnology, University of Groningen, The Netherlands
1993 Joined the Norwegian University of Life Sciences (NMBU), Ås, Norway
1997 Appointed Professor of Biochemistry, NMBU
2016 Member, The Norwegian Academy of Science and Letters
About the Novonesis Biotechnology Prize
The Novonesis Biotechnology Prize recognises outstanding research or technological achievements that contribute to the development of innovative and sustainable biotechnology solutions for the benefit of people and the planet.
The Prize is awarded annually by the Novo Nordisk Foundation and is accompanied by:
– DKK 4.5 million research grant
– DKK 0.5 million personal award
– DKK 0.5 million for hosting an international symposium
Further information
Norwegian University of Life Sciences (NMBU)
Communications Office
+47 6494 9000
[email protected]
Vincent Eijsink – Institutional Contact
Faculty of Chemistry, Biotechnology and Food Science
Norwegian University of Life Sciences (NMBU), Ås, Norway
[email protected]
Novo Nordisk Foundation:
Christian Mostrup,
Director, Public Relations
+45 3067 4805
[email protected]
