Immobilization Of Lipase Research Articles

Rebuilding the lid region from conformational and dynamic features to engineering applications of lipase in foods: Current status and future prospects.

The applications of lipases in esterification, amidation, and transesterification have broadened their potential in the production of fine compounds with high cumulative values. Mostly, the catalytic triad of lipases is covered by either one or two mobile peptides called the "lid" that control the substrate channel to the catalytic center. The lid holds unique conformational allostery via interfacial activation to regulate the dynamics and catalytic functions of lipases, thereby highlighting its importance in redesigning these enzymes for industrial applications. The structural characteristic of lipase, the dynamics of lids, and the roles of lid in lipase catalysis were summarized, providing opportunities for rebuilding lid region by biotechniques (e.g., metagenomic technology and protein engineering) and enzyme immobilization. The review focused on the advantages and disadvantages of strategies rebuilding the lid region. The main shortcomings of biotechnologies on lid rebuilding were discussed such as negative effects on lipase (e.g., a decrease of activity). Additionally, the main shortcomings (e.g., enzyme desorption at high temperatre) in immobilization on hydrophobic supports via interfacial action were presented. Solutions to the mentioned problems were proposed by combinations of computational design with biotechnologies, and improvements of lipase immobilization (e.g., immobilization protocols and support design). Finally, the review provides future perspectives about designing hyperfunctional lipases as biocatalysts in the food industry based on lid conformation and dynamics.

Sortase-mediated immobilization of Candida antarctica lipase B (CalB) on graphene oxide; comparison with chemical approach

In this study, Candida antarctica lipase B (CalB) was covalently immobilized on the surface of graphene oxide (GO) nanoparticles by sortase-mediated immobilization as well as a chemical attachment approach. Sortase is a transpeptidase that provides one-step purification and targeted immobilization of CalB from one specific site, presenting oriented attachment of the enzyme to a solid support. Chemical immobilization, on the other hand, is considered as a random immobilization, in which the protein can bind to the support from different regions of the protein surface. In this approach, amine-functionalized GO was further modified with glutaraldehyde to facilitate the covalent binding of CalB via its amine residues. The applied methods produced 60% and 100% immobilization yields and presented 0.106 U/mg and 0.085 U/mg of specific activities for the oriented and random immobilization, respectively. The stabilized enzyme with the sortase-mediated approach retained approximately 80% of its initial activity at 50°C.

Recent developments of lipase immobilization technology and application of immobilized lipase mixtures for biodiesel production

AbstractLipases are considered the most widely used industrial biocatalysts, and play a significant role in diverse industrial and biotechnological applications such as in biodiesel. Biodiesel is a renewable and ecologically friendly biofuel, and has received significantly increased attention in recent years. The reaction media of biodiesel synthesis via the transesterification process of fats and oils could be considered cascade reactions. The use of a mixture of immobilized lipases as biocatalysts in biodiesel reactions has received much consideration since it is a ‘greener technique’ and has several advantages over free lipases. The selection of appropriate carrier materials and immobilization techniques fundamentally affects the immobilized lipases’ catalytic performance for biodiesel production. Hence, this review discusses the recent developments for carrier materials and techniques for lipase immobilization as well as the current status of immobilized lipases mixtures and their application for biodiesel synthesis. The initial part of this review presents a brief introduction of lipases and their application for biodiesel preparation. New carrier materials and different basic and recent lipase immobilization techniques are also evaluated. Most significantly, studies carried out on mixtures of immobilized lipase‐catalyzed biodiesel for the last 15 years (2006–2021) are summarized. The economic and environmental evaluation of enzymatic biodiesel production is also presented. In the future, the application of mixed and co‐immobilized lipases may be enlarged to other enzymes and processes. © 2022 Society of Chemical Industry and John Wiley & Sons, Ltd

LIPASES: AN EFFICIENT BIOCATALYST FOR BIOTECHNOLOGICAL APPLICATIONS

Lipases (3.1.1.3) are ubiquitous, biogenic enzymes which hydrolyses the triacylglycerols at the water-oil interface. Many species of animals, plants, and microbes produces lipases. The organisms able to produce lipases which could tolerate organic solvents, high temperature, is of industrial interest. Apart from its natural aqueous catalysis it also performs synthetic reactions in non-aqueous conditions, which have undergone tremendous development in last decade and have become a part of growing biotechnological applications. Immobilization of lipases on the particulate carriers have also been widely used for the enzyme’s efficient use. Vast industrial applications have been established such as detergent formulations, oleochemical, nutrition, textile, agrochemical industry, food technology, pharmaceutical field and fine chemical processing. Except latter three, most commercial applications do not requisite excessive purification or high degree of purity.

Production and characterization of biodiesel from canola oil through enzymatic transesterification

Abstract Biodiesel, a promising type of biofuel, can be produced from various types of renewable feedstocks, ranging from animal fats to plant oil. It is mainly made up of fatty acid alkyl ester compounds due to the transesterification reaction. This work aims to synthesize and characterize biodiesel, known as fatty acid methyl esters, from canola oil using an enzymatic reaction involving immobilized Novozym 435 and Rhizomucor miehei (RM IM) lipase enzymes.4 g of canola oil was added to the reaction mixture consisting of 0.2 g immobilized lipase and 3:1 methanol to oil ratio. First, the enzymatic methanolysis reaction was conducted at the temperature of 35°C and at agitation rate of 216 rpm for 24 hours. Next, the synthesized biodiesel was characterized using the Gas Chromatography-Mass Spectroscopy (GC/MS) analysis. Based on the analysis results, the main fatty acid methyl esters present in both products were hexadecanoic acid, 9-octadecenoic acid (z)-, 9,12,15-octadecatrienoic acid, (z, z, z)-, and 11,14-eicosadienoic acid. The transesterification of canola oil using both enzymes consistently revealed methyl oleate as the methyl ester with the highest composition, ranging from 67 to 71 %. In conclusion, canola oil was successfully converted into fatty acid methyl ester via the enzymatic transesterification process in this study.

Activation and Stabilization of Lipase B from Candida antarctica by Immobilization on Polymer Brushes with Optimized Surface Structure

A reusable support system for the immobilization of lipases is developed using hybrid polymer-inorganic core shell nanoparticles. The biocatalyst core consists of a silica nanoparticle. PMMA is grafted from the nanoparticle as polymer brush via ARGET ATRP (activator regenerated by electron transfer atom transfer radical polymerization), which allows defining the surface properties by chemical synthesis conditions. Lipase B from Candida antarctica is immobilized on the hybrid particles. The activity and stability of the biocatalyst are analyzed by spectroscopic activity analysis. It is shown that the hydrophobic PMMA brushes provide an activating surface for the lipase giving a higher specific activity than the enzyme in solution. Varying the surface structure from disordered to ordered polymer brushes reveals that the reusability of the biocatalyst is more effectively optimized by the surface structure than by the introduction of crosslinking with glutaraldehyde (GDA). The developed immobilization system is highly suitable for biocatalysis in non-native media which is shown by a transesterification assay in isopropyl alcohol and an esterification reaction in n-heptane.

Development of organic porous material from pineapple waste as a support for enzyme and dye adsorption

The transformation of agricultural wastes such as pineapple waste into valuable product such as biochar will be of great advantage. Biochar is a black carbon produced by pyrolysis which can act as good adsorbent for organic substances due to the high porosity characteristic. Due to the instability and the non-recyclability factor of free enzymes, the use of immobilized enzyme is getting more attraction. Furthermore, biochar or activated carbon (AC) has been widely used in industries to adsorb pollution such as dye. In this study, process pyrolysis was used to convert pineapple waste biomass (PWB) into useful adsorbent such as biochar (BC) and activated carbon (AC) for lipase immobilization and RBBR dye adsorption. Several steps such as impregnation of PWbB with nitric acid, and process pyrolysis of pineapple waste at various temperatures and residence time have been performed. Studies of characterization of biochar such as Thermogravimetric analysis (TGA), Brunauer – Emmett – Teller (BET), Fourier Transform Infra-Red (FTIR) and Scanning Electron Microscopy (SEM) were accomplished to analyze the differences in performance. The performance of BC in lipase immobilization and RBBR dye adsorption were investigated by varying parameters i.e. initial concentration, physical size of PWB (grounded and non-grounded pineapple waste (PW) biomas) and physical size of BC (crushed and non-crushed BC). The achievements of generated BC were compared with commercial AC. The result shows the highest amount of protein adsorbed during immobilization was achieved at F500 1 h PWbB (92.99%). Meanwhile, the maximum dye removal was achieved at F 600.5 h PWbB (83.59%). Adsorption kinetics studies insinuate that the overall process follows the pseudo-first-order where the process was influenced by intraparticle and film diffusion while equilibrium isotherm studies is best described by Langmuir isotherm models. As a conclusion, the conventional liability burden of pineapple waste is possible to be transformed into valuable commodity especially for waste treatment.

(Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study

The present work reports on the use of a hybrid blend of biopolymers as a matrix for lipase immobilization. (Hydroxypropyl)methyl cellulose (HPMC) and Chitosan (CS) were combined in order to formulate a film on which Mucor miehei lipase was immobilized. The biocatalyst was studied upon the model reaction of propyl laurate synthesis. The system was examined in terms of its capability to provide an appropriate environment where lipase will maintain its activity. The ratio of the polymers used was examined and HPMC:CS=2:1 proved to form the most promising matrix. Increasing the amount of the immobilized enzyme appears to improve the reaction yield indicating, however, mass transfer limitations. Apparent activation energy was calculated and energy input showed that ultra-sonication accelerated the initial rate of the reaction. Different reaction solvents were tested with isooctane being the most effective. The enzyme-containing film showed a remarkable reusability, since it can be used for up to 35 times without loss of activity. Finally, Atomic Force Microscopy (AFM) was performed to observe the morphology of the most promising films. The HPMC/CS film exhibits a nanostructure without a unique characteristic length and a roughness of 42.8 nm while the presence of enzyme smoothens the film as the roughness decreases to 5.5 nm.

PRODUCTION, PURIFICATION AND IMMOBILIZATION OF TRIACYLGLYCEROL LIPASE FROM INDIGENOUS LIPOLYTIC MICROORGANISMS

Triacylglycerol lipase was produced from locally isolated Aspergillus niger and Bacillus sp. using submerged fermentation. The process was optimized and lipase was purified and immobilized. Maximum lipase activity was obtained; with microorganisms cultured in medium containing 1% olive oil and 1% soybean meal as substrate, 72hrs incubation at 30°C, pH 6.0 and medium supplementation with 2% glucose, 1% peptone for A. niger, 72hrs incubation at 37°C, pH 8.0 and medium supplementation with 1% glucose, 1.5% peptone for Bacillus sp. The enzymes were purified using ammonium sulphate precipitation and ion exchange chromatography to achieve 13-14 fold purity with a yield ranging from 53-57%. Lewatite and Amberlite were found to be very good supports for the immoblization of bacterial and fungal lipases, respectively. The immobilization of lipase was proved to be an excellent tool for industrial applications of the enzyme.

Characteristics of Crosslinking Polymers Play Major Roles in Improving the Stability and Catalytic Properties of Immobilized Thermomyces lanuginosus Lipase.

This study aimed to improve the stability and catalytic properties of Thermomyces lanuginosus lipase (TLL) adsorbed on a hydrophobic support. At the optimized conditions (pH 5 and 25 °C without any additions), the Sips isotherm model effectively fitted the equilibrium adsorption data, indicating a monolayer and the homogenous distribution of immobilized lipase molecules. To preserve the high specific activity of adsorbed lipase, the immobilized lipase (IL) with a moderate loading amount (approximately 40% surface coverage) was selected. Polyethylenimine (PEI) and chitosan (CS) were successfully applied as bridging units to in situ crosslink the immobilized lipase molecules in IL. At the low polymer concentration (0.5%, w/w) and with 1 h incubation, insignificant changes in average pore size were detected. Short-chain PEI and CS (MW ≤ 2 kDa) efficiently improved the lipase stability, i.e., the lipase loss decreased from 40% to <2%. Notably, CS performed much better than PEI in maintaining lipase activity. IL crosslinked with CS-2 kDa showed a two- to three-fold higher rate when hydrolyzing p-nitrophenyl butyrate and a two-fold increase in the catalytic efficiency in the esterification of hexanoic acid with butanol. These in situ crosslinking strategies offer good potential for modulating the catalytic properties of TLL for a specific reaction.

Lipase catalyzed green epoxidation of oleic acid using ultrasound as a process intensification method

Epoxidized fatty acids are important green intermediates for chemical industry. This work was focused on the direct epoxidation of oleic acid (OA) using immobilized lipase Novozym® 435 as the catalyst and hydrogen peroxide (HP) as the epoxidation agent. The impacts of reactant molar ratio (HP:OA = 1…2), reaction temperature (30–60 °C), catalyst loading (7 wt-%) and stirring rate (500–1000 rpm) on the fatty acid conversion and epoxide selectivity were evaluated Acoustic irradiation and an advanced stirring system were implemented for reaction intensification and different ultrasound amplitudes (0–90%) were screened. Novozym® 435 revealed to be an efficient and durable catalyst for fatty acid epoxidation. The reaction was promoted by an excess of HP. The highest epoxide selectivity was about 80% at full conversion of oleic acid reached within 200 min. Ultrasound irradiation (90% amplitude) enhanced the initial reaction rate by a factor two compared to silent conditions and higher oleic acid conversions were reached compared to silent experiments. The catalyst preserved its activity and selectivity rather well, which was confirmed by catalyst recovery experiments conducted in the absence and presence acoustic irradiation. The main ring-opening agent is the fatty acid itself, which resulted in the formation of esters.

Immobilization of Thermomyces lanuginosus lipase via ionic adsorption on superparamagnetic iron oxide nanoparticles: Facile synthesis and improved catalytic performance

The present work describes a simple, rational, and optimized methodology for the immobilization of lipase from Thermomyces lanuginosus (TLL) via ionic adsorption on non-commercial superparamagnetic iron oxide nanoparticles (SPIONs). First, the surface loads of both the enzyme and nanoparticles were evaluated by zeta potential measurements over a wide pH range. In addition, the loading surface of TLL was mapped computationally using the information obtained from the Protein Data Bank (PDB) under three different pH conditions. This information allowed to conduct the directional immobilization of the lipase on the surface of the SPIONs in order to maximize the lipase–SPION interaction and keep the enzyme’s active sites facing the solution. TLL was immobilized at a low ionic strength (5 mmol L–1) on the SPIONs under optimized conditions (sodium acetate buffer, pH 4, 25 °C using an initial enzyme loading of 30 mg per gram of support). Under such conditions, almost full immobilization (99.49% adsorption capacity) was observed. The prepared biocatalyst retained 62.3% of its hydrolytic activity relative to the initial activity of the free lipase. Maximum catalytic efficiency (or acid conversion percentage) of 80% in decyl oleate synthesis performed in a solvent-free system was observed after 12 consecutive cycles of reaction of 180 min each. In addition, the lipase–nanoparticle interaction was also evaluated by fluorescence spectroscopy and the thermodynamic parameter values ΔGo=-25.8kJmol-1, ΔHo=-10.44kJmol-1, and, ΔSo=0.122kJmol-1K-1 were found, which is consistent with the occurrence of predominantly ionic interactions. These results clearly show the promising use of the prepared biocatalyst to catalyze decyl oleate production, an ester with emollient properties, in an eco-friendly process (solvent-free system).

Immobilization of Lipases on Modified Silica Clay for Bio-Diesel Production: The Effect of Surface Hydrophobicity on Performance

The hydrophobicity of a support plays a critical role in the catalytic efficiency of immobilized lipases. 3-aminopropyltriethoxysilane (APTES)-modified silica clay (A-SC) was coupled with silane coupling agents of different alkyl chains (methyl triethoxysilane, vinyl triethoxysilane, octyl triethoxysilane, and dodecyl triethoxysilane) to prepare a series of hydrophobic support for lipase immobilization. The lipases were immobilized onto the support by conducting glutaraldehyde cross-linking processes. The results showed that the activity of the immobilized biocatalyst increased with hydrophobicity. The hydrolytic activity of Lip-Glu-C12-SC (contact angle 119.8°) can reach 5900 U/g, which was about three times that of Lip-Glu-A-SC (contact angle 46.5°). The immobilized lipase was applied as a biocatalyst for biodiesel production. The results showed that the catalytic yield of biodiesel with highly hydrophobic Lip-Glu-C12-SC could be as high as 96%, which is about 30% higher than that of Lip-Glu-A-SC. After being recycled five times, the immobilized lipase still maintained good catalytic activity and stability. This study provides a good strategy to improve the efficiency of immobilized lipases, showing great potential for future industrial application on biodiesel production.

Lipases: Sources of Acquisition, Ways of Production, and Recent Applications

Enzymes are extensively used in biotechnological processes in several areas of industry. They are sustainable and safe, and their specificity is another characteristic that improves the performance in the process. Among enzymes, lipase is relevant due to the ability to play different roles in the industry and the possibility of collecting them from microbial sources that are found in industrial residues. This can reduce the costs of enzyme production. In relation to that, lipase immobilization is an interesting process that allows the enzymes to be reused and improves enzyme robustness. Among them, the cross-linked enzyme aggregates (CLEAs) methodology is attractive due to its simplicity, low cost (given the absence of support), and greater interaction with the substrate. Thus, in this review, we discussed the potential of lipase. We reviewed the traditional and new sources of obtaining lipases, along with the ways of improving production, activity, and application in the industry.

Incorporation of metallic particles in activated carbon used in lipase immobilization for production of isoamyl acetate

AbstractBACKGROUNDBiotechnology has revolutionized the use of enzymes for application in industrial processes. The present work evaluated the effect of functionalizing activated carbon with metallic nanoparticles obtained from corn cob residue on lipase immobilization. The aim was to improve the enzymatic activity of the immobilized enzyme and subsequent application of derivatives in the synthesis of isoamyl acetate ester (banana flavor).RESULTSThe activated carbon (CCAC) had a mesoporous structure and specific surface area of 1135 m2 g−1, characteristic of supports from precursor material with a high cellulose content, which was reduced in metalized carbon (CCACM) due to the insertion of metallic particles (760 m2 g−1). CCACM showed a slightly higher lipase absorptive capacity than CCAC (280.72 ± 0.27 mg g−1 and 276.46 ± 0.03 mg g−1, respectively). Furthermore, for derivatives the optimal reaction medium conditions were pH 7.0 and 30 °C, confirming the advantage associated with lipase immobilization, obtaining activity values of 84.0 ± 2.12 U, 72.3 ± 1.7 U and 31.4 ± 1.9 U, for lipase immobilized on CCACM, CCAC and native form, respectively. The derivatives showed potential application in the synthesis of isoamyl acetate ester, with conversions above 90% and stability during five cycles of use.CONCLUSIONThe activated carbon metallization process showed an increase in lipase immobilization efficiency and proved to be a promising support, since there was an increase in its enzymatic activity and the derivatives obtained showed potential application in aroma synthesis, reaching conversion above 90%. © 2022 Society of Chemical Industry (SCI).

Lipase immobilization on multi-walled carbon nanotubes used as a target fishing tool and followed by molecular docking technique to analyze lipase inhibitor from Robinia pseudoacacia L.

In this study, R. pseudoacacia flowers exhibited potential lipase (Aspergillus niger) inhibitory activity. To quickly explore the active compound, ligand fishing was adopted for screening the ligand from R. pseudoacacia flowers by lipase immobilized on magnetic polyamidoamine dendrimer-coated multi-walled carbon nanotubes. After ligand fishing, the target compound was separated purposefully by optimizing the separation conditions of high-speed counter-current chromatography (HSCCC). As results, kaempferol with the IC50 of 327.64 ± 15.33 μg/mL was separated and identified. The further molecular docking results indicated that kaempferol was interacted with amino acid residue in the active site of lipase through van der Waals force, hydrogen bonds and Pi-Pi T-shaped interactions, yielding the binding energy of − 6.43 kcal/mol. The present method not only revealed the lipase inhibitory substances in R. pseudoacacia, but also provided an effective means for the screening of other natural substances.

Purification and Optimization of Extracellular Lipase from a Novel Strain Kocuria flava Y4.

The exogenous lipolytic activities of Kocuria sp. have been recognized earlier but the genus further contains many more unexplored strains. In this study, the extracellular lipase activity of Kocuria flava Y4 (GenBank accession no. MT773277), isolated from Dioscorea villosa during our previous study, was regulated by different physicochemical parameters, such as pH, temperature, shaking speed, and incubation time. For efficient immobilization of the extracellular lipase, 4% sodium alginate, 50 mL of 25 nM CaCl2.2H2O solution, and 15 min. Hardening time of gel beads in calcium chloride was used. For the first time, K. flava Y4 lipase was purified using ammonium sulphate precipitation followed by dialysis and DEAE-Sepharose anion exchange chromatography with Sepharose-6B gel filtration chromatography, yielding ∼15-fold purified lipase with a final yield of 96 U/mL. The SDS-PAGE of purified lipase displayed a single strong band, indicating a monomeric protein of 45 kDa. At a temperature of 35°C and pH 8, the purified lipase showed maximum hydrolytic activity. Using p-nitrophenyl acetate (p-NPA) as the hydrolysis substrate, the values of Km and Vmax derived from the Lineweaver–Burk plot were 4.625 mM and 125 mol/min−1mg−1, respectively.

Improved synthesis of dietary triglycerides by using lipase supported on clay carriers.

In the search for healthier and more functional foods, dietary triglycerides (TAGs) have played a prominent role in the food industry. The objective of this work was to evaluate new clay supports to immobilize lipase from Rhizopus oryzae and use it in the synthesis of TAGs. The immobilization of lipase by physical adsorption was carried out, determining the hydrolytic activity, esterification, immobilization yield, thermal stability, and kinetic and thermodynamic parameters. Afterwards, acidolysis was carried out and the product characterized as to composition, acidity index (AI), peroxide index (PI), and analysis of the sn-2 position. The mean hydrolytic activity of free lipase was 23,568.43±559.20 Ug-1 and for lipase immobilized in acidified kaolin and diatomite, 1409.04±51.07 and 1235.67±9.56Ug-1 ; immobilization yield of 23.78% and 20.21% and esterification activity of 1827.99 and 1722.66Ug-1 , respectively, maintaining more than 60% of the relative activity after 8 h of incubation at different temperatures. The reaction using the derivative immobilized in acidified diatomite resulted in the degree of incorporation (DI) 41.53%±3.99%. From the results, the potential of diatomite and kaolin as support in the immobilization of lipase for the synthesis of dietary TAGs was verified.

Nanomaterial-immobilized lipases for sustainable recovery of biodiesel – A review

In recent years, the development and deployment of nano-immobilized lipases, as robust biocatalysts, has appeared a promising alternative for biodiesel production. There is a significant hike in using nano-sized support matrices for enzyme-based biotransformation bioprocesses with ever-increasing scientific awareness and nanotechnological advancement. Several nano-scale materials include magnetic and non-magnetic nano-particles, silica nano-particles, carbon nanotubes, graphene/graphene oxide, electrospun nanofibers, metal–organic frameworks, and other nanohybrid matrices are of supreme interest that can shield the catalytic attributes of enzymes after immobilization. Furthermore, nano-sized support matrices immobilized enzymes also offer numerous advantages that native enzymes fail to display on their own, such as high catalytic efficacy, high catalytic turnover, induced stability under harsh reaction conditions, high resistivity against reaction by-products (which otherwise can hinder/inhibit the pristine enzyme), low mass transfer limitation, and high yield under mild processing environment. Lipases are considered principal candidates (biocatalysts) for biodiesel production via transesterification processes, among several industrially relevant enzymes. The nano-immobilized lipases showed a broader working range under different pH and temperature conditions, a highly requisite challenge in indusial settings. Herein, we reviewed several perspectives of sustainable biodiesel production using nano-immobilized lipases. First, following a brief introduction, this review is spotlighting numerous existing and state-of-the-art strategies for lipase immobilization on nanomaterials. Second, the critical factors that characterize nano-biocatalysts are discussed to show the need for optimal reaction conditions to further sustainable transformation. Third, promising nano-carriers to develop lipase-based nanobiocatalyst are given with suitable examples. Fourth, some influential factors that improve the overall performance of nano-immobilized lipases are discussed in terms of the sustainability and processability of the entire production process. Lastly, the contemporary challenges and key considerations for sustained biodiesel production from waste resources are also given for future studies.

Waste Management in the Agri-Food Industry: The Conversion of Eggshells, Spent Coffee Grounds, and Brown Onion Skins into Carriers for Lipase Immobilization.

One of the major challenges in sustainable waste management in the agri-food industry following the “zero waste” model is the application of the circular economy strategy, including the development of innovative waste utilization techniques. The conversion of agri-food waste into carriers for the immobilization of enzymes is one such technique. Replacing chemical catalysts with immobilized enzymes (i.e., immobilized/heterogeneous biocatalysts) could help reduce the energy efficiency and environmental sustainability problems of existing chemically catalysed processes. On the other hand, the economics of the process strongly depend on the price of the immobilized enzyme. The conversion of agricultural and food wastes into low-cost enzyme carriers could lead to the development of immobilized enzymes with desirable operating characteristics and subsequently lower the price of immobilized enzymes for use in biocatalytic production. In this context, this review provides insight into the possibilities of reusing food industry wastes, namely, eggshells, coffee grounds, and brown onion skins, as carriers for lipase immobilization.