Available online at www.sciencedirect.
com
Application prospects and opportunities of inorganic
nanomaterials for enzyme immobilization in the food-
processing industry
Hao Wu 1,2 and Wanmeng Mu 2,3
Enzymes seem to be ideal biocatalysts in various bioprocessing
fields due to their eco-friendliness and nonhazardous merits.
Generally, enzymological characteristics such as catalytic
activity, selectivity, specificity, and stability often become weak
in extreme processing conditions. Enzymes immobilized onto
support materials through the physical, chemical, and
physicochemical mechanisms can overcome these limitations.
Compared with macroscopic supports, inorganic nanomaterials
show great superiority in enzyme immobilization due to their
specific physicochemical properties, such as large surface
area, pore diameter, mechanical resistance, and so on. Herein,
this paper mainly talks about recent advances in enzyme
immobilization employing representative nanomaterials,
including silica-based nanomaterial, carbon-based
nanomaterial, metal-based nanomaterial, and magnetic
nanomaterial. The prospective and opportunities of these
materials applied in the food-processing industry are also
discussed to promote immobilization technological innovation.
Addresses
1
School of Food Science and Bioengineering, Changsha University of
Science & Technology, Changsha 410114, China
2 mobilized enzyme is not easy to move freely in the ac­
State Key Laboratory of Food Science and Technology, Jiangnan
University, Wuxi, Jiangsu 214122, China
3
International Joint Laboratory on Food Safety, Jiangnan University,
Wuxi, Jiangsu 214122, China
Corresponding author: Wanmeng Mu (wmmu@jiangnan.edu.cn),
Current Opinion in Food Science 2022, 47:100909
This review comes from a themed issue on Food Engineering &
Processing
Edited by Martin Scanlon
For complete overview of the section, please refer to the article
collection, “Food Engineering & Processing 2022”
Available online 4th August 2022
https://doi.org/10.1016/j.cofs.2022.100909
2214-7993/© 2022 Elsevier Ltd. All rights reserved.
Introduction
With people paying more and more attention to en­
vironmental protection, natural enzyme biocatalysts
have widely received great attention from various in­
dustries, such as food, medicine, textile, feed, fine
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]]
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chemicals, and environmental protection, with their
milder condition, higher efficiency, and greener catalytic
superiority over traditional chemical catalysts [1–5].
However, the free enzymes often suffered from extreme
reaction conditions such as strong acids/bases, high
temperature, and organic reagents during the biopro­
cessing, thus destroying the conformational structure of
enzyme and resulting in poor catalytic activity and op­
erational stability [6–8]. Besides, other inevitable draw­
backs for free enzymes, such as the high production cost,
poor operation stability, difficulty in reusing, and re­
cycling, also to some extent, greatly hinder their in­
dustrial applications broadly. To meet the requirements
for enzymes with an excellent catalytic performance by
industries, several mature methods, including protein
engineering, chemical modification, and immobilization
technology, are adopted to enhance the catalytic activity
and operational stability [9,10]. Among them, im­
mobilization technology shows unparalleled advantages
in heterogeneous catalytic reactions and overcomes the
drawbacks of recyclability [11–13]. Besides, the im­
tion system, and the thermal and pH stability is often
enhanced, therefore, prolonging its half-life in the long-
term reaction process. In addition, the protein en­
gineering technology could be combined with enzyme-
immobilization methods to better improve the enzyme
properties.
Typically, enzymes can be immobilized on support
material through different manners from reversible
physical adsorption and ionic linkages to irreversible
entrapment, covalent bonds, and cross-linking based on
different attachment modes of enzymes to carriers [14]
(Figure 1). The physical adsorption process is relatively
much easier, simpler, and cheaper than other methods,
and can furthest retain the original activity of the en­
zyme, but the binding force is weak, which will cause
enzyme leakage. This disadvantage can be overcome by
covalent bonds and cross-linking because the enzyme
can be tightly bound to the support material and less
possibility of the resulting enzyme leakage. Never­
theless, the activity of the enzyme may be reduced if the
active site or conformation of the enzyme is affected
[15]. Besides, the immobilization uniformity and protein
orientation were determined by the functional groups of
enzymes.
Current Opinion in Food Science 47( 2022) 100909
2 Food Engineering & Processing
Figure 1
The different methods of enzyme immobilization and their respective properties.
The selection and type of support material are critical
both for immobilization and purification of enzymes
because the strength of enzyme-support interaction will
affect the binding and releasing of enzymes [17]. The
ideal support material usually possesses the following
characteristics: (i) the support material is cheap and en­
vironmentally friendly; (ii) the support material has a
large specific surface area, a good pore structure, and an
easily modified surface; (iii) the support material has
good mechanical stability and is easy to recycle and
reuse [18,19••]. To develop immobilized enzymes with
good operation stability and high catalytic efficiency,
researchers have made great attempts to select various
materials as support materials, from the conventional
supports such as glass, natural polymers, alginate, and
macroporous resin, diatomite to various nanomaterials
(nanostructured materials) nowadays [20]. The proper
coordination between different types and characteristics
of nanomaterials and the enzymes is very important for
the immobilization process because the activity of the
immobilized enzymes may be reduced due to structural
changes [17]. Compared with traditional large-size ma­
terials, nanomaterials have a special quantum size and
quantum tunneling effect, showing excellent properties
in sound, light, magnetism, electricity, and heat [3••]. In
addition, its large specific surface area and easily mod­
ified surface enable high enzyme-loading capacity per
mass unit and minimal resistance to substrate diffusion,
gaining more attention from scientific researchers [21].
Nonetheless, the application of inorganic nanomaterials
Current Opinion in Food Science 47( 2022) 100909
Current Opinion in Food Science
for enzyme immobilization still faces challenges, such as
leaching, denaturation, and low transfer efficiency
[22••]. And these inorganic nanomaterials must be
modified by some functional groups on the surface to
better immobilize enzymes. Also, the properties of the
reactive groups in the support will affect the enzyme-
support multipoint covalent immobilization process [7].
With the development of nanoscience and technology,
many functional nanomaterials have penetrated all walks
of life, including those used for enzyme immobilization,
bringing new impetus to the technological innovation
and development of various industries. This review
mainly introduces the common methods of enzyme-im­
mobilization strategy and their respective advantages
and disadvantages. Synchronously, the application of
some representative new nanomaterials, such as silica-
based nanomaterial, carbon-based nanomaterial, metal-
based nanomaterial, and magnetic nanomaterial in en­
zyme immobilization, is summarized (Figure 2), and the
application prospect and development opportunity of
these nanomaterials in the food-processing industry are
also discussed extensively [22••].
Silica-based nanomaterial for enzyme
immobilization
Silica-based nanomaterials (MCM-41, MCM-48, SBA-
15, etc.) represented by silica (SiO2) are widely used in
immobilizing enzymes due to their characteristics of
high specific surface area, pore structure, controllable
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 Inorganic nanomaterials for enzyme immobilization Wu and Mu
Figure 2
Different inorganic nanomaterials based on enzyme immobilization.
pore diameter, and morphology, good stability, non­
toxicity, and functionalizable surface [23]. The meso­
porous silica (mSiO2) (mesoporous silica nanoparticles
composed of Si–O–Si framework of inorganic silicon) is
the most thoroughly studied and most mature material
known at present. There are large numbers of pore
structures in the structure of mSiO2 with a size of
2–50 nm, making it possess many characteristics of na­
nomaterials. In addition, these inorganic silicon nano­
particles can increase the properties of organic
nanomaterials after hybridizing, such as optics, chemical
stability, and biocompatibility, by introducing functional
organic-group molecules on the surface [19••,24•]. For
instance, after organic functionalization using silane-
coupling reagents, the modified SBA-15 supported
Thermomyces lanuginosus lipase that exhibited reasonable
glycerolysis activity and good operational stability [25].
Mesoporous silica nanomaterials have also been reported
to be used to immobilize lipase, glucose oxidase (GOx),
and horseradish peroxidase [26]. The immobilization
effect of mesoporous silica material is also affected by
the properties of the material itself, such as material
aperture, particle size, and specific surface area, which
will play an important role in the amount of enzyme
loading. The ideal mesoporous material of enzyme im­
mobilization needs to reach an equilibrium point be­
tween enzyme loading, pore diameter, and pore-gap
ratio. It has been reported that the pore diameter of
mesoporous silica material larger than the enzyme has a
better immobilization effect. Currently, mesoporous
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3
Current Opinion in Food Science
silica nanomaterials are more used in immobilizing
single enzymes. With the rise and wide application of
multi-enzyme-coupling catalytic reaction, it remains a
challenge in achieving ordered assembly (or self-as­
sembly) of multiple enzymes on mesoporous silica sur­
faces.
Carbon-based nanomaterial for enzyme
immobilization
Carbon-based nanomaterials (such as graphene, carbon
nanotubes (CNTs), etc.) have been widely used in the
field of enzyme immobilization owing to their excellent
properties of good thermal conductivity, high-tempera­
ture resistance, chemical inertness, and good bio­
compatibility [27,28]. However, a single carbon-based
nanomaterial used for enzyme immobilization also has
some disadvantages, such as poor material toughness,
poor dispersibility, and low efficiency. Therefore, to
expand the wide application of carbon-based nanoma­
terials, many researchers attempt to prepare carbon-
based nanocomposites to overcome the shortcomings of
a single carbon-based nanomaterial. Graphene oxide
(GO), a derivative of graphene, has a high specific sur­
face area and good biocompatibility. Its surface contains
many functional groups, such as carboxyl, hydroxyl,
carbonyl, and epoxy groups, making it an ideal carrier for
enzyme immobilization. The enzyme can be im­
mobilized onto GO by interacting with these functional
groups through noncovalent bonds or covalent coupling.
However, GO displays strong hydrophilic properties,
and that leads to difficulty recovering and reusing from
Current Opinion in Food Science 47( 2022) 100909
4 Food Engineering & Processing
an aqueous solution when used as an immobilized ma­
terial. Jiang et al. [29] modified the Fe3O4 magnetic
nanoparticles (MNPs) with an amino group and then
covalently linked it to the carboxylic acid of GO to ob­
tain a GO–CO@NH–Fe3O4 magnetic nanocomposite
that was applied to immobilize trypsin. The results
showed that the amount of immobilized enzyme could
reach 0.275 mg/mg, and the enzyme activity could still
retain 84% after storage at 4°C for 1 month, and the
stability was greatly improved.
On the other hand, as one-dimensional hollow tubes
consisting of nanoscale diameter in the forms of single-
walled or multiwalled CNTs, CNTs have many unique
properties such as good electrical conductivity, strong
adsorption capacity, and good biocompatibility. Also,
these properties can be strengthened by functionalizing
its surface to better improve the immobilization effi­
ciency of enzymes [19••]. For example, it prevented the
aggregation of multiwalled CNTs in an aqueous solution
and enhanced its affinity with lipase after using po­
tassium permanganate to modify the surface via non­
aggressive oxidation [19••]. Choi [30] dispersively
oxidized multiwalled CNTs in perfluorinated sulfonic
acid (Nafion) solution to form CNT@Nafion nano­
composites, and then covalently fixed GOx and laccase
on microporous structures of their surfaces that were
pretreated by plasma corrosion, greatly improving the
immobilization efficiency. When using the CNTs for
enzyme immobilization, the toxic effects on health and
the food industry should also be considered because
pure powdered CNT form may be hazardous, which is a
critical step for its application.
Metal–organic frameworks for enzyme
immobilization
Metal–organic framework (MOFs) is composed of metal
nodes and organic ligands connected by coordination
bonds. The topological structure and properties of
MOFs can be adjusted according to their multiple metal
nodes and ligands, making it possible to regulate the
interaction between MOFs and enzymes [31]. Com­
pared with traditional immobilized enzyme carriers with
uncontrollable pore size, high preparation cost, enzyme
leaching, and poor product stability, MOFs have the
advantages of higher specific surface area and pore vo­
lume, controllable pore size, and thermal stability
[31,32]. Currently, the synthesis strategies of en­
zyme–MOF composites mainly include surface im­
mobilization, covalent bonding, pore entrapment, and in
situ synthesis [33]. According to the order of synthesis,
the synthesis strategies of the enzyme–MOF complex
can be divided into two categories: post-synthetic
packaging and de novo encapsulation [33]. Post-synthetic
packaging mainly involves the synthesis of MOFs first,
and then immobilization of enzymes onto MOFs by
Current Opinion in Food Science 47( 2022) 100909
surface adsorption, covalent cross-linking, or pore dif­
fusion. De novo encapsulation, also known as in situ
synthesis, is to add enzymes to metal ion precursors and
organic ligand solutions and obtain enzyme–MOFs after
dispersion, crystal growth, purification, and drying [34].
Owing to the diversity in the structure and properties of
different enzymes and MOFs, the choice of im­
mobilization methods should be carefully considered to
differentiate design based on the pore structure of en­
zymes and MOFs. The immobilized enzymes onto
MOFs can form nanoscale composite materials. Com­
pared with enzymes immobilized by macroscopic mate­
rials, nanoparticles have better catalytic and sensing
properties and are widely used in biosensing and en­
vironmental pollutant purification. Thus far, the enzyme
immobilization using MOFs is mainly focused on laccase
for wastewater treatment [19••,35,36]. The application
of MOF-based materials used in the food-processing
industry is insufficient, which should be further
strengthened and developed.
Magnetic nanomaterial for enzyme
immobilization
MNPs not only have the advantages of large surface
area, high mechanical strength, and easy chemical
modification, but also possess unique magnetic proper­
ties, having a wide application in magnetically targeted
drug delivery, biological imaging, immunosensing de­
tection, and enzyme immobilization [24•,37••]. Espe­
cially, the enzyme immobilized by MNPs can be easily
recovered and reused from the aqueous solution if
adding an external magnetic field [38]. The lipase im­
mobilized on zinc-doped magnetic iron oxide nano­
particles could retain over 50% of its initial catalytic
activity after recyclability for twenty cycles for fish oil
hydrolysis [39]. However, MNPs contain lesser active
groups on the surface and are easy to be oxidized when
exposed to air. Furthermore, the magnetic attraction
between MNPs facilitates the aggregation of magnetic
particles, which affects the activity and dispersion
properties of immobilized enzymes, resulting in poor
immobilization efficiency when only using MNPs as
carriers.
Some studies try to modify its surface by introducing
some active functional groups, including carboxyl, hy­
droxyl, and amino, to improve the immobilization effi­
ciency. Hu et al. modified the MNPs with 3-
aminopropyl triethoxysilane to immobilize alkaline pro­
tease, and the results showed that the recovery rate of
the immobilized enzyme could reach 54.2%, and the
relative activity of the immobilized enzyme remained
79.9% and 50.1% after 5 and 10 batches, respectively
[40]. Among many MNPs, Fe3O4 nanoparticles have the
advantages of simple preparation, low toxicity, and good
biocompatibility, and are one of the widely used MNPs.
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 Table 1

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The nanomaterial used for enzyme immobilization and its various applications.

Enzyme Nanomaterial Immobilization Enhancement (compared with the free enzyme) Application References
method
Lipase MNPs Covent binding Retaining over 50% activity after recyclability for Fish oil hydrolysis [39]
twenty cycles; 1.5 times higher selectivity for
docosahexaenoic acid.
Lipase Phenyl–SBA-15 Physical adsorption Improves operational stability, retains 95.21% Synthesis of diacylglycerol [25]
activity after five cycles of reuse, and produces
higher diacylglycerol content.
Lipase Chitosan–SBA-15 hybrid Covalent binding Exhibits excellent enzymology properties, retains Improvement of enzyme [42]
nanomaterial 85% activity after ten cycles, and shows better properties
thermal stability and storage stability.
Lipase Polyoxometalate–MOFs Encapsulation Retains 90.4% activity after five catalytic Esterification of [43]
rounds, retains 80% yield after eight reuses. cinnamic acid
Galactose oxidase CNTs Physical adsorption CNTs can serve as a platform for functional Biosensor for galactosemia [44]
biosensors.
Laccase GO Covalent binding Retains over 75% activity after six cycles. Biodegradation of azo dyes [45]
in colored wastewater
Cellulase MNPs Physical adsorption Enhances catalytic activity, retains 15.5% yield of Hydrolysis of cellulose [46]
glucose after three cycles.
Glucose oxidase CNTs Physical adsorption CNTs can serve as a platform for glucose Biosensor for glucose [47]
biosensors.
Nitrile hydratase Fe3O4@mSiO2 Covalent binding Exhibits excellent enzymology properties, retains Synthesis of nicotinamide [48]
29.74% yield of nicotinamide after seven cycles of
reaction.
Pectinase Chitosan–MNPs Covalent binding Retains 85% activity after twenty-five batch cycles in Fruit juice clarification [49]
orange juice clarification, shows high
thermostability.
Acid protease, pectinase, and laccase Fe3O4@SiO2–NH2 Physical adsorption Exhibits excellent activity and stability, shows high Sludge dewatering [41]
efficiency and stable sludge dewatering
performance.
Inorganic nanomaterials for enzyme immobilization Wu and Mu

Current Opinion in Food Science 47( 2022) 100909

5
6 Food Engineering & Processing
In addition, it can also be modified by SiO2, MOFs, and
GO, to prepare Fe3O4@SiO2, Fe3O4@MOFs, and
Fe3O4@GO functional composite nanomaterials. The
preparation of functional composite MNPs has become a
research trend. Wan et al. immobilized three enzymes,
including acid protease, pectinase, and laccase on
Fe3O4@SiO2–NH2 by electrostatic interaction, and used
them for sludge dewatering [41]. The results showed
that the immobilized enzymes endowed high efficiency
and stable sludge dewatering performance in a wide pH
range. Nonetheless, there are still some challenges in the
research of MNPs, such as using magnetic nanomaterials
for co-immobilization of multiple enzymes and system­
atically studying the interaction mechanism and binding
sites between MNPs and enzymes (Table 1).
Challenges and outlooks
Recent advancements in nanoscience and technology
have led to the new emerging nanomaterials for enzyme
immobilization, having made great progress in the field
of biosensing, biomedicine, food processing, and en­
vironmental pollution. Nanomaterials hold good bio­
compatibility, high specific surface area, and easily
modified surface. These properties are beneficial for
improving the load of immobilized enzymes and main­
taining the stability of the enzyme, showing a good ap­
plication prospect. However, the use of a single
nanomaterial will also have disadvantages of low im­
mobilization efficiency and difficult separation from an
aqueous solution. The preparation of nanocomposite
materials is helpful to overcome these weaknesses, such
as the development of MNPs@GO. Nonetheless, there
are still some problems to be solved in the preparation of
nanocomposites, such as the high costs and complicated
steps during preparation. Second, the surface modifica­
tion of nanocomposites with complexity may reduce the
activity of enzymes. How scientifically selecting the
appropriate material (such as the appropriate aperture,
types of nanocomposites) is also an important factor for
the design of an efficient immobilized carrier. Third, the
interaction between nanomaterials and enzymes as well
as the binding site remains to be further studied, which
will help in better design and engineer the desired na­
nomaterials or enzymes to balance the catalytic activity,
selectivity, specificity, and stability between them. In
addition, the potential safety issues of nanomaterials in
the field of food processing need to be considered, be­
cause some pure powdered nanomaterials (such as
CNTs) may be hazardous to human health. The solution
to these problems will help accelerate the industrial
application of the technology of nanomaterial-im­
mobilized enzymes. In the food-processing industry, the
nanomaterial-immobilized enzyme is mainly focused on
the immobilization of lipase, GOx, and amylase. Other
food-processing enzymes should also be got insights
using nanomaterial-immobilization technology to reduce
Current Opinion in Food Science 47( 2022) 100909
production costs and accelerate the development of the
food-processing industry.
CRediT authorship contribution statement
Hao Wu: Writing – original draft, Writing – review and
editing. Wanmeng Wan: Project administration.
Conflict of interest statement
The authors declare that they have no known competing
financial interests or personal relationships that could
have appeared to influence the work reported in this
paper.
Acknowledgements
This work was funded by the National Natural Science Foundation of
China (No. 31922073).
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