Study for Enzyme Catalyzed Hydrogels for Smart Applications

Zeyu Li

1,* a

, Xianyang Wen

and Xuantong Yi

School of Chemistry and Chemical Engineering, Shihezi University, Shihezi, Xinjiang, 832003, China

Leeds College, Southwest Jiaotong University, Chengdu, Sichuan, 611756, China

Mapleleaf International School, Dalian, Liaoning, 116650, China

Keywords: Enzyme-Catalyzed Hydrogels, Assembly Mechanisms, Regulatory Strategies, Biomedical Applications,

Challenges and Prospects.

Abstract: Hydrogels, as three-dimensional hydrophilic polymer networks capable of absorbing significant amounts of

water, hold immense potential in biomedicine, tissue engineering, and drug delivery. This paper highlights

enzyme-catalyzed hydrogels as precision biomaterials that utilize enzymatic reactions—such as oxidation,

dephosphorylation, and transglutaminase bonding—for spatiotemporally controlled assembly. Their

substrate-specific catalysis achieves over 90% conversion efficiency under physiological conditions (37°C,

pH 7.4), enabling rapid gelation in less than 60 seconds with minimal cytotoxicity (95% cell viability in 3D

cultures). Despite these advantages, clinical translation faces several challenges: free enzymes lose 40-60%

activity within 72 hours in biological environments, production costs for therapeutic-grade enzymes exceed

$1,000 per gram, and the mechanical strength (typically less than 50 kPa compressive modulus) remains

inadequate for load-bearing tissues. Recent advancements in enzyme technology involve covalent enzyme

immobilization on silica nanoparticles (enhancing thermal stability by 15°C) and on graphene oxide

composites, which triple tensile strength. Multi-enzyme systems now facilitate glucose-responsive drug

release with a responsiveness of less than 30 minutes. Emerging applications extend beyond biomedicine to

environmental engineering, including peroxidase-mediated pollutant degradation, achieving 85% phenol

removal in 6 hours, and catalase-based biosensors for pathogen detection. Future priorities involve the

development of intelligent systems that integrate diagnostic triggers (e.g., protease-activated fluorescence)

with therapeutic functions, while also enhancing enzyme reusability (exceeding 50 cycles) and standardizing

biocompatibility protocols. Interdisciplinary innovation is essential to balance material performance with

scalable production for both clinical and environmental applications.

1 INTRODUCTION

Hydrogels, being soft materials with distinctive

characteristics, have drawn extensive attention in

recent scientific research. These materials are typified

by a three-dimensional network structure, which

imparts them with an outstanding capacity to absorb

a substantial amount of water, exhibits remarkable

application potential in diverse fields such as

biomedicine, tissue engineering, and drug delivery.

Enzyme-catalyzed hydrogels are formed and

constructed via enzymatic reactions, endowing

hydrogels with unique properties and precise

regulatory abilities. As biological catalysts, enzymes

https://orcid.org/0009-0002-7708-3556

https://orcid.org/0009-0001-7052-2125

https://orcid.org/0009-0008-1181-5893

possess advantages like high efficiency, specificity,

and mild reaction conditions. They can enable the

controllable assembly of hydrogels within complex

biological systems, thereby meeting the requirements

of different application scenarios. In-depth

investigation into the assembly and regulation

mechanisms of enzyme-catalyzed hydrogels is of

great significance for promoting their practical

applications across various fields. This article

explains the assembly mechanisms and regulation of

Enzyme-Catalyzed Hydrogels. Then, some

applications and future development are mentioned in

this article.

510

Li, Z., Wen, X. and Yi, X.

Study for Enzyme Catalyzed Hydrogels for Smart Applications.

DOI: 10.5220/0013828500004708

Paper published under CC license (CC BY-NC-ND 4.0)

In Proceedings of the 2nd International Conference on Innovations in Applied Mathematics, Physics, and Astronomy (IAMPA 2025), pages 510-515

ISBN: 978-989-758-774-0

2 ASSEMBLY MECHANISMS OF

ENZYME-CATALYZED

HYDROGELS

2.1 Enzyme-Mediated Covalent Cross-

Linking Mechanisms

Enzymatic cross-linking (a process where enzymes

catalyze the formation of covalent bonds between

polymer chains to create three-dimensional networks)

relies on redox (reduction-oxidation reactions

involving electron transfer) or transferase reactions

(enzyme-catalyzed reactions that transfer functional

groups between molecules) to construct covalent

hydrogel networks (water-swollen polymer networks

linked by irreversible chemical bonds). Horseradish

peroxidase (HRP) (a heme-containing enzyme that

oxidizes substrates using hydrogen peroxide as an

electron acceptor), a well-characterized redox

enzyme, catalyzes the oxidation of phenolic

derivatives (aromatic compounds containing

hydroxyl groups attached to a benzene ring) in the

presence of hydrogen peroxide (H₂O₂). Specifically,

HRP oxidizes phenolic hydroxyl groups in modified

polysaccharides (e.g., dextran or hyaluronic acid) to

highly reactive quinones (oxidized aromatic

compounds with conjugated carbonyl groups) . These

quinones subsequently undergo Michael addition (a

reaction between a nucleophile and an α,β-

unsaturated carbonyl compound) or Schiff-base

reactions (formation of imine bonds between amines

and carbonyl groups) with nucleophilic groups

(electron-rich groups such as -NH₂ or -SH that donate

electrons to form bonds), forming stable covalent

bonds and a three-dimensional network. For instance,

Carnes et al. (2020) demonstrated that HRP-

crosslinked fibrin scaffolds exhibit compressive

moduli of 15–20 kPa, closely mimicking the

mechanical properties of native cartilage extracellular

matrix (ECM). Such scaffolds support chondrocyte

adhesion and proliferation, achieving >90% cell

viability after 7 days, thus highlighting their potential

in cartilage tissue engineering.

Tyrosinase (a copper-dependent oxidase enzyme

that catalyzes phenolic group oxidation), another

significant redox enzyme, can catalyze the oxidation

of substrates containing phenolic groups to quinones,

subsequently triggering cross-linking reactions. In the

preparation of biocompatible hydrogels, tyrosinase

can oxidize polymers or small molecule gelling

agents modified with tyrosine residues (amino acid

residues containing phenolic side chains). The formed

quinones react with nucleophilic groups in the system,

leading to the cross-linking of hydrogels. This cross-

linking method holds potential application value in

areas such as wound dressings and tissue adhesives,

as it can effectively promote wound healing and

tissue repair.

Transglutaminase (TG) (an enzyme that catalyzes

the formation of ε-(γ-glutamyl)lysine isopeptide

bonds between glutamine and lysine residues), a

transferase, catalyzes isopeptide bond formation (a

covalent bond between the γ-carboxamide group of

glutamine and the ε-amino group of lysine) between

glutamine and lysine residues. Yang et al. (2024)

engineered a TG-crosslinked fibrin-polypeptide

hydrogel that upregulated cardiac-specific genes (e.g.,

TNNT2 and MYH6) by 2.3-fold compared to non-

enzymatic controls. This system provides a

mechanically robust scaffold for cardiac tissue

regeneration.

2.2 Enzyme-Triggered Supramolecular

Assembly Mechanisms

Phosphatases within the hydrolase family are

instrumental in the formation of supramolecular

hydrogels. Supramolecular hydrogels are formed

through enzyme-modulated non-covalent interactions,

such as hydrophobic effects or hydrogen bonding,

thereby triggering the self-assembly of small-

molecule gelling agents. For example, Wang et al.

(2020) discovered that alkaline phosphatase can

dephosphorylate Fmoc-tyrosine phosphate,

increasing its hydrophobicity and facilitating the self-

assembly of Fmoc-tyrosine into nanofibers, which in

turn induces hydrogelation. This mechanism holds

broad application prospects in fields such as

biosensors and drug delivery carriers, enabling the

precise detection of biomolecules and the controlled

release of drugs.

The matrix metalloproteinase (MMP) family

plays critical roles in tumor microenvironment

regulation, with MMP-7 emerging as a key

therapeutic target due to its overexpression in

malignant tumors. Building on this property, Tanaka

et al. (2015) developed an MMP-7-responsive

peptide-lipid precursor system. This innovative

design leverages enzyme-specific hydrolysis to

trigger molecular structural transformation: the

precursor substances release gelators with self-

assembly ability under the action of MMP-7, forming

a three-dimensional network structure within cancer

cells. This hydrogelation strategy based on the

response of matrix metalloproteinases provides novel

ideas and methods for cancer treatment, with the

potential to achieve the precise killing of cancer cells.

Study for Enzyme Catalyzed Hydrogels for Smart Applications

511

Thermolysin promotes the self-assembly process

by catalyzing the formation of covalent bonds in

substrates within aqueous solutions through reverse

hydrolysis reactions. Wang et al. (2020) utilized

thermolysin to prepare in-situ amphiphilic Fmoc-

tripeptide hydrogelators for cell culture applications.

This enzyme catalyzes substrate reactions under mild

conditions, resulting in a hydrogel that demonstrates

excellent biocompatibility, thereby presenting a novel

material option for cell culture.

To address the detection of bacterial resistance,

the action of β-lactamase, the hydrogelator is released

and self-assembles to form a supramolecular

hydrogel. During this process, the incorporation of

cephalosporin hydrolysis sites as molecular switches

allows these systems to release hydrogelators upon

contact with β-lactamase secreted by resistant

bacteria, thereby forming physical barriers through

self-assembly. This approach enables visual detection

of drug-resistant pathogens via gelation, while the

sustained drug release prolongs localized

antimicrobial effects, offering new methods and

approaches for biological detection and the research

and development of antibacterial drugs.

DNA polymerases play a key role in the

construction of DNA-based supramolecular

hydrogels, which synergize biomolecular precision

with enzymatic catalysis. The formation of DNA

hydrogels depends on the specific base pairing

between DNA molecules and enzymatic reactions.

Their structure and properties can be precisely

regulated by adjusting the DNA sequence and

reaction conditions. Such hydrogels hold potential

application value in the biomedical field, such as in

cell culture, drug delivery, and bioimaging. These

values indicate the future research directions for

enzyme-catalyzed hydrogels.

Enzyme-triggered supramolecular hydrogels

exploit the catalytic specificity of enzymes—such as

phosphatases, MMP-7, thermolysin, β-lactamase, and

DNA polymerases—to achieve spatiotemporal

control over gelation. By harnessing enzymatic

dephosphorylation, hydrolysis, or reverse hydrolysis,

these systems modulate molecular interactions (e.g.,

hydrophobicity, covalent bonding, or programmable

DNA assembly) to drive self-assembly into

functional networks. Such mechanisms enable

innovative biomedical applications, including tumor-

targeted therapy, bacterial resistance detection, and

stimuli-responsive drug delivery, highlighting their

transformative potential in precision biomedicine and

smart material design.

3 REGULATORY STRATEGIES

OF ENZYME-CATALYZED

HYDROGELS

3.1 Modulation via Enzyme

Concentration and Activity Control

Enzyme concentration plays a pivotal role in the

gelation kinetics of hydrogels (Sun et al. 2019). In

horseradish peroxidase (HRP)-catalyzed systems,

increasing HRP concentration from 0.008 to 0.5

mg/mL reduces gelation time from 60 to 5 seconds,

with constant polymer and hydrogen peroxide

concentrations (Park et al., 2011). However,

excessively high enzyme concentrations can lead to

rapid reactions that are challenging to control and

may adversely affect the hydrogel's network structure,

impacting properties like swelling behavior and

biocompatibility.

3.2 Substrate Engineering for Tailored

Hydrogelation

In hydrogel assembly, the characteristics of the

constituent polymeric precursors, herein referred to as

substrates, are of critical importance. Factors such as

the type of polymer employed, its molecular weight

(MW), and the specific functional groups present

within its structure significantly dictate the assembly

process and the resultant hydrogel properties.

Modification of these substrate parameters allows for

the tailoring of the final hydrogel's physical and

chemical characteristics. In cartilage tissue

engineering, selecting different polysaccharides or

proteins as substrates and introducing specific

functional groups can modulate mechanical strength,

degradation rate, and biocompatibility

(Khanmohammadi, Jalessi, & Asghari, 2022).

In the supramolecular enzyme-driven hydrogel

system, the design of substrates determines the

release and self-assembly behavior of gelling agents.

Designing substrates sensitive to specific enzymes

enables the specific response of hydrogels.

Shigemitsu et al. (2020) focused on the development

of non-enzymatic protein-responsive soft materials.

They integrated an enzyme-sensitive supramolecular

hydrogel with a protein-triggered enzyme activation

system. By designing enzyme-activity triggers

(EATs), they could convert non-enzymatic protein

inputs into enzymatic activity, achieving controlled

protein release. These results underscore a key

advantage of tailored hydrogelation: the ability to

design composite systems with highly specific,

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programmable responses. The successful integration

of an enzyme-sensitive hydrogel with protein-

triggered enzyme activation demonstrated controlled

protein release specifically in response to biomarker

proteins, highlighting the significant potential of this

tailored approach for advanced applications like

stimulus-responsive drug delivery.

3.3 Environmental Impacts on

Assembly Kinetics

Environmental factors such as temperature, pH value,

and ionic strength have a substantial impact on the

assembly process of enzyme-catalyzed hydrogels (Li

et al. , 2022; Tian et al. , 2025).

Temperature variations significantly affect

assembly, primarily by modulating enzyme activity

and the kinetic energy of reacting molecules. Within

an optimal range specific to the enzyme, increasing

temperature generally accelerates the enzymatic

reaction rate and molecular movement, thus

facilitating faster hydrogel formation. However,

temperatures exceeding this optimal range can lead to

irreversible enzyme denaturation and inactivation,

thereby inhibiting or preventing hydrogelation.

pH is another critical environmental parameter.

Most enzymes exhibit maximal activity within a

narrow, optimal pH range. As highlighted by studies

on systems like tyrosinase-catalyzed hydrogels (Song

et al., 2021; Choi et al., 2018), deviations from this

optimal pH can markedly reduce the enzyme's

catalytic efficiency. This directly impacts the

hydrogel formation rate and can influence the

structural quality and final properties of the hydrogel

network. Furthermore, changes in pH value can alter

the protonation state of ionizable functional groups on

both the enzyme and the substrates or gelling agents.

This modification of charge states affects electrostatic

interactions, solubility, and self-assembly behavior.

Consequently, careful selection and control of pH,

tailored to the specific enzyme system and application

requirements, are essential for successful and

reproducible hydrogel assembly.

Ionic strength also plays a significant role in

hydrogel assembly. Ions in the solution interact with

charged residues on enzymes, substrates, and gelling

agents, influencing their conformation, solubility, and

intermolecular forces (e.g., electrostatic screening or

bridging). In certain enzyme-catalyzed systems, the

type and concentration of ions can critically modulate

the assembly rate and the mechanical properties of the

resulting hydrogel.

4 APPLICATIONS OF ENZYME-

CATALYZED HYDROGELS IN

THE BIOMEDICAL FIELD

4.1 Tissue Engineering

In the realm of tissue engineering, enzyme-catalyzed

hydrogels are crucial for creating an optimal

microenvironment that supports essential cellular

functions like proliferation, migration, and

differentiation, which are vital for applications such

as bone fracture repair and wound healing. Zhang et

al. (2025) synthesized a Cellulose-CD-MMT

hydrogel with a compressive strength of up to 2.19

MPa and high affinity for pollutants. This hydrogel-

like structure can potentially mimic the extracellular

matrix. For instance, its mesoporous structure, similar

to those in tissue-engineering hydrogels, can enhance

cell-nutrient interactions. Also, its biocompatibility,

as evidenced by no significant toxicity to L929 mouse

fibroblast cells at 6-15 mg/mL, indicates its potential

to support cell growth and differentiation, thus

facilitating tissue repair and regeneration.

Supramolecular enzyme-driven hydrogels also

possess unique advantages in tissue engineering. By

designing substrates sensitive to specific enzymes,

the in-situ formation of hydrogels in the body can be

achieved, enabling better adaptation to the complex

structure and physiological requirements of tissues.

This in-situ formed hydrogel can closely integrate

with the surrounding tissues, reducing immune

responses and enhancing the tissue repair effect (Cao

et al., 2021). For example, by using phosphatase-

responsive hydrogel precursors, under the action of

phosphatases at specific tissue sites in the body, the

hydrogel can form in-situ, providing immediate

support for tissue repair.

4.2 Cancer Treatment and Imaging

Enzyme-catalyzed hydrogels demonstrate great

potential in cancer treatment and imaging. In cancer

treatment, in-situ self-assembling enzyme-catalyzed

hydrogels enable precise targeting of cancer cells and

their efficient killing. Enzymes overexpressed in the

tumor microenvironment, such as alkaline

phosphatase and esterase, can trigger the self-

assembly of hydrogel precursors(Kim et al., 2023;

Tan et al., 2015). The formed hydrogels can

encapsulate drugs and deliver them to cancer cells.

This targeted delivery strategy can increase the drug

concentration at the tumor site, minimize damage to

normal tissues, and enhance the treatment effect.

Study for Enzyme Catalyzed Hydrogels for Smart Applications

513

In cancer imaging, imaging technologies based on

enzyme-catalyzed hydrogels can achieve highly

sensitive and specific detection of tumors. By

designing hydrogel precursors combined with

imaging agents, under the action of tumor-related

enzymes, the hydrogels self-assemble and

accumulate at the tumor site, thereby amplifying the

imaging signal. For example, in photoacoustic

imaging, the self-assembly of hydrogel precursors

containing photoacoustic probes triggered by tumor-

specific enzymes can significantly enhance the

photoacoustic signal at the tumor site, enabling

precise positioning and imaging of tumors(Xu et al.,

2021).

5 CURRENT CHALLENGES AND

LIMITATIONS

Despite significant advancements in the field of

enzyme-catalyzed hydrogels, several challenges and

limitations persist. The stability and availability of

enzymes remain critical constraints for their broad

application. Enzymes are prone to inactivation during

storage and use, particularly in complex biological

environments, where their activity is influenced by

numerous factors. Additionally, the production cost

of certain enzymes is high, and the extraction and

purification processes are intricate, restricting their

large-scale application. To address these issues, novel

enzyme immobilization techniques and stabilization

methods need to be developed to enhance the stability

and reproducibility of enzymes while reducing

production costs.

The mechanical properties of some hydrogels

require further improvement to meet the demands of

diverse application scenarios. In certain tissue

engineering applications that necessitate

withstanding substantial mechanical loads, such as

bone tissue repair, the existing enzyme-catalyzed

hydrogels may be incapable of providing sufficient

support strength. It is imperative to optimize the

formulation and preparation process of hydrogels,

introduce reinforcing materials, or improve the cross-

linking method to enhance the mechanical properties

of hydrogels.

Furthermore, the paucity of in-vivo research

impedes the clinical translation of enzyme-catalyzed

hydrogels. Currently, there is insufficient in-depth

understanding of the long-term stability of hydrogels

in the body, the safety of degradation products, and

their interactions with surrounding tissues. It is

essential to strengthen in-vivo experimental research,

establish appropriate animal models, and thoroughly

explore the behavior and action mechanisms of

hydrogels in the body in order to provide a solid

theoretical foundation for their clinical applications.

6 CONCLUSION

The assembly and regulation of enzyme-catalyzed

hydrogels represent a highly potential and promising

research area, demonstrating broad application

prospects in multiple fields, particularly biomedicine.

Through the application of multi-dimensional

understanding and refined research methods to

further explore the assembly mechanisms and

regulatory strategies of enzyme-catalyzed hydrogels,

hydrogel materials with specific properties and

functions can be designed and fabricated to meet the

full range of biomedical fields such as tissue

engineering, drug sustained-release, cell culture and

other different subdivisions. Although some

challenges currently exist, with the interdisciplinary

integration of material science, biotechnology,

medicine, and other disciplines, solutions to these

problems are anticipated.

In the future, research on enzyme-catalyzed

hydrogels will progress towards greater intelligence,

personalization, excellent stability and high

efficiency. New enzyme-catalyzed systems and

intelligent responsive hydrogels will be further

developed to achieve microscopic precise modulation

of hydrogel properties and accurate responses to

biological signals. For example, designing hydrogels

capable of simultaneously responding to multiple

biomarkers to enable precise diagnosis and treatment

of complex diseases. Simultaneously, efforts will be

intensified in in-vivo research and clinical translation,

and a comprehensive and scientific evaluation system

of multidimensional indicators will be established to

promote the transition of enzyme-catalyzed

hydrogels from laboratory research to clinical

applications, thereby making more significant

contributions to human health. Additionally,

expanding the applications of enzyme-catalyzed

hydrogels in other fields, such as biosensors and

environmental remediation, will present new

opportunities and prosperity into technology iteration

and industrial upgrading in these related fields

ACKNOWLEDGEMENTS

All the authors contributed equally and their names

were listed in alphabetical order.

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