Enzyme Technology Research Articles

Enzyme technology in bioethanol production from lignocellulosic biomass: Recent trends with a focus on immobilized enzymes

Enzyme immobilization is a useful tool to produce biocatalysts with improved performance, such as high activity, high stability at operational conditions, and easy recovery and reuse. In this context, the production of second-generation ethanol using immobilized enzymes was reviewed. Emphasis was placed on the pre-treatment and/or hydrolysis steps to increase efficiency and reduce the cost of the process. In addition, the process design of bioethanol using immobilized enzymes was critically reviewed. In the enzymatic pre-treatment, laccases, manganese peroxidases, lignin peroxidases, and lytic polysaccharide monooxygenases are the main enzymes involved. When considering processes with heterogeneous biocatalysts, laccases are the most explored enzyme. In the hydrolysis step, cellulases and hemicellulases or a mixture of them are the main enzymes explored in the literature frequently using magnetic nanoparticles as support for enzyme immobilization. Although enzyme immobilization is a mature technology, the use of these biocatalysts is frequently limited to only one step of the bioethanol production process, such as pre-treatment or hydrolysis performed using Benchmark Technology. However, some recent papers have explored innovative design processes using a mixture of immobilized enzymes or co-immobilized enzymes to join some process steps, thereby decreasing the cost of enzymes and equipment.

Cleaner and sustainable synthesis of high-quality monoglycerides by use of enzyme technologies: techno-economic and environmental study for monolaurin

Currently, monoglycerides (MG) are produced using a complicated energy-intensive technology that contributes negatively toward greenhouse gas mitigation. This work suggests a cleaner and simpler one-step enzymatic production of α-monolaurin in an inert membrane reactor, where the reaction and enzyme separation are conducted simultaneously in one unit. Candida antarctica lipase (Lipozyme 435) was used to catalyze the esterification reaction between lauric acid and glycerin in a solvent-free system under mild temperatures. Response surface methodology was used to optimize the reaction conditions. The optimal conditions were a molecular sieve of 14.85% w/w, a temperature of 56.95 °C, an enzyme amount of 5.38% w/w, and a molar ratio of 4.75% w/w. The gas chromatography (GC) analysis showed that the α-monolaurin percentage was 49.5% when the enzymatic process (ENZ) was used. The conventional chemical (CHEM) and autocatalytic (AUT) esterification methods were also performed to study their proportional MG yields. The GC results showed the MG percentages of 43.9 and 41.7% for CHEM and AUT, respectively. Economic analysis was also conducted for the suggested enzymatic technique, and the findings were compared with those of the CHEM and AUT technologies. Using a plant capacity of 4950 t/year and 11% interest for the proposed ENZ process, the total capital investment of α-monolaurin production was preferably four times less than that of the CHEM process and three times less than that of the AUT method, presenting investment possibilities. However, the ENZ process showed the least profitability (net profit per day) among the three processes. Nevertheless, the return on investment and net present value for the ENZ process were preferably higher than those of CHEM and AUT because of its interestingly lower inside battery limit plant cost and less energy consumption. The AUT/CHEM processes generated a total carbon dioxide (CO2) exhaust of 678.7 t CO2 eq./year. In contrast, the ENZ process exhausted a total CO2 of only 50 t CO2 eq./year. The present integrated techno-economic and environmental study of α-monolaurin production emphasizes the green and cost benefits of the proposed ENZ technology.Graphical

Biosensor for PCR amplicons by combining split trehalase and DNA-binding proteins: A proof of concept study

The use of polymerase chain reaction (PCR) technology in low-cost settings has gained significant attention due to its ability to amplify and detect specific bacterial pathogen genes, aiding in the diagnosis of infectious diseases. PCR amplicons can be visualized by conventional endpoint agarose gel electrophoresis and fluorochrome-enabled real-time PCR. However, this is not practical in on-field tests due to cumbersome instrumentation, labor-intensive reaction preparation, and long time-to-results. Many studies have combined microfluidic devices or electrochemical dyes with PCR technology to enhance in-field operability. However, the high cost of manufacturing high-precision microfluidic chips and the dependence on non-portable readout equipment limit their further development. In this paper, we present a proof-of-principle study of a novel method combining split enzyme technology and DNA-binding proteins for the convenient and efficient detection of amplified genetic material from bacterial pathogens. The amplicon binding split trehalase assay (ABSTA) relies on incorporating specific recognition sequences of DNA-binding protein SpoIIID in tandem within one of the PCR primers. Applied by a Gram-type specific PCR assay, ABSTA was capable of discriminating Staphylococcus devriesei and Escherichia coli in <90 min after colony PCR amplicons bound split trehalase fragments-fused SpoIIID and triggered split enzyme complementation. The salt concentration, protein reagents versus DNA substrate ratio, direction and linker length of tandem recognition sites required for the complementation were optimized. The glucose produced by restored enzymatic activity was detectable by glucometer. With limited requirements for reaction preparation and the compatibility of ABSTA with commercially available handheld glucometers, this test platform has substantial potential to be implemented into a future point-of-care (POC) diagnostic tool for detecting pathogen specific genes with further improvement.

Nanotechnology and enzyme immobilization: a review

The synergy between enzymes and nanotechnology (nano-biocatalysts) has created some of the most promising biomaterials fabricated by synergistically incorporating advanced nano-biotechnology. The incorporation of enzymes into nanotechnology is of great significance for making nanomaterials that are rarely harmful to the environment. However, the unique/specific physicochemical characteristics and supramolecular nature ascribed to functional nanostructures (nanomaterials), have made them novel, interesting, and exceptional matrices for the creation of nano-biocatalysts. These have a lot of potential for improving the enzyme stability, function, efficiency, kinetic characteristics, vulnerability to diffusional constraints, and engineering performance in bioprocessing. Hence, the nano-biocatalysts developed contain exceptional properties with many potential applications in diverse fields. This review covers a wide range of the nanotechnology and enzyme technology involved in producing nano-biocatalysts, including different mechanisms, strategies in nanomaterial enzyme immobilization, and various nanocarriers, as well as recent developments in controlling enzyme activity. The vast range of potential applications of nano-biocatalysts in various fields, including food, pharmaceuticals, biofuels, and bioremediation, has been discussed.

Applications of Enzyme Technology to Enhance Transition to Plant Proteins: A Review.

As the plant-based food market grows, demand for plant protein is also increasing. Proteins are a major component in foods and are key to developing desired structures and textures. Seed storage proteins are the main plant proteins in the human diet. They are abundant in, for example, legumes or defatted oilseeds, which makes them an excellent candidate to use in the development of novel plant-based foods. However, they often have low and inflexible functionalities, as in nature they are designed to remain densely packed and inert within cell walls until they are needed during germination. Enzymes are often used by the food industry, for example, in the production of cheese or beer, to modify ingredient properties. Although they currently have limited applications in plant proteins, interest in the area is exponentially increasing. The present review first considers the current state and potential of enzyme utilization related to plant proteins, including uses in protein extraction and post-extraction modifications. Then, relevant opportunities and challenges are critically discussed. The main challenges relate to the knowledge gap, the high cost of enzymes, and the complexity of plant proteins as substrates. The overall aim of this review is to increase awareness, highlight challenges, and explore ways to address them.

Study of some parameters and Partial purification of prolidase from serum women preeclampsia

This study was carried out by partial purification of prolidase from blood serum patients with preeclampsia by ion exchange The degree of purification enzyme (1. 85) fold, enzyme yield (8.82) and specific activity is (8.88) IU/mg .The kinetic studies of partially purified The enzyme technology demonstrated the optimal substrate concentration which was (97) mmol/L and Vmax (71.42 )(U/L),km(1.25) while optimal The optimum temperature was (37°C) and pH (9.2). molecular The weight of the partially purified enzyme was determined by a gel Electrophoresis method, in the presence of polyacrylamide gel and sodium Dodecyl Sulfate (SDS_PAGE) which showed that the approximate. The molecular weight was (54KD). We found a high level of Erythropoietin hormone in Pre-eclampsia patients which was a significant (P≤0.01) increase, (438.47 ) when she was in Control (251.70 ), the value of antidiuretic hormone in the patient was a significant (P≤0.05) increase (7.343) while in Control decrease value (2.155), the value of the ALD hormone in the patient was a significant decrease (P≤0.05) (288.7) and control was (143.6), Nitric Oxide in the patient was a significant (P≤0.05) (30.0) and control was increase (44.2) and vitamin D in the patient was a significant decrease (P≤0.05) (11.04) and control was(15.78) We conclude from the above results that there are some variables that rise with preeclampsia, such as the hormone ADH and the hormone EPO, but other variables such as ALD, vitamin D3 and nitric oxide decrease with increased pregnancy pressure, that is, with preeclampsia, in addition to that the main objective of the research is to purify the prolidease enzyme in the serum of women with preeclampsia and to know the duration of its effect This enzyme on pregnant women and linked it in another study with materials to find a new treatment

Special Issue: Application of Proteomics and Enzyme Technologies in Foods

This Special Issue entitled “Application of Proteomics and Enzyme Technologies in Foods” explores the latest progress and perspectives on the development and application of enzyme technologies, proteomics, and bioprocessing in the context of food science [...]

Using Exonucleases for Aptamer Characterization, Engineering, and Sensing.

ConspectusAptamers are short, single-stranded nucleic acids that have been selected from random libraries to bind specific molecules with high affinity via an in vitro method termed systematic evolution of ligands by exponential enrichment (SELEX). They have been generated for diverse targets ranging from metal ions to small molecules to proteins and have demonstrated considerable promise as biorecognition elements in sensors for applications including medical diagnostics, environmental monitoring, food safety, and forensic analysis. While aptamer sensors have made great strides in terms of sensitivity, specificity, turnaround time, and ease of use, several challenges have hindered their broader adoption. These include inadequate sensitivity, bottlenecks in aptamer binding characterization, and the cost and labor associated with aptamer engineering. In this Account, we describe our successes in using nuclease enzymes to address these problems. While working with nucleases to enhance the sensitivity of split aptamer sensors via enzyme-assisted target recycling, we serendipitously discovered that the digestion of DNA aptamers by exonucleases is inhibited when an aptamer is bound to a ligand. This finding served as the foundation for the development of three novel aptamer-related methodologies in our laboratory. First, we used exonucleases to truncate nonessential nucleotides from aptamers to generate structure-switching aptamers in a single step, greatly simplifying the aptamer engineering process. Second, we used exonucleases to develop a label-free aptamer-based detection platform that can utilize aptamers directly obtained from in vitro selection to detect analytes with ultralow background and high sensitivity. Through this approach, we were able to detect analytes at nanomolar levels in biological samples, with the capacity for achieving multiplexed detection by using molecular beacons. Finally, we used exonucleases to develop a high throughput means of characterizing aptamer affinity and specificity for a variety of ligands. This approach has enabled more comprehensive analysis of aptamers by greatly increasing the number of aptamer candidates and aptamer-ligand pairs that can be tested in a single experiment. We have also demonstrated the success of this method as a means for identifying new mutant aptamers with augmented binding properties and for quantifying aptamer-target affinity. Our enzymatic technologies can greatly streamline the aptamer characterization and sensor development process, and with the adoption of robotics or liquid handling systems in the future, it should be possible to rapidly identify the most suitable aptamers for a particular application from hundreds to thousands of candidates.

Sustainable bioconversion of synthetic plastic wastes to polyhydroxyalkanoate (PHA) bioplastics: recent advances and challenges

Millions of tons of chemical plastics are accumulated annually worldwide in terrestrial and marine environments due to inadequate recycling plants and facilities and low circular use. Their continuous accumulation and contamination of soil and water pose a severe threat to the environment and to human, animal and plant health. There is therefore an urgent need to develop effective eco-environmental strategies to overcome the significant environmental impacts of traditional plastic waste management practises (incineration, landfilling, and recycling). In recent years, reports on microbial strains equipped with the potential of degrading plastic materials, which can further be converted into usable products such as PHA bioplastics have sprung up, and these offer a possibility to develop microbial and enzymatic technologies for plastic waste treatment and then progressing plastics circularity. In this chapter, an overview of the reported microbial and enzymatic degradations of petroleum-based synthetic plastics, specifically polyethylene, polystyrene, polypropylene, polyvinyl chloride, polyurethane and polyethylene terephthalate, is detailed. Furthermore, the harvesting of depolymerization products to produce new PHA materials with high added industrial value can be considered as an innovative solution, helping to increase synthetic plastic recycling rate and creating new circular economy opportunities. Finally, the challenge of ending plastic pollution is still difficult, but sustainable, renewable, bio-based and completely biodegradable, PHA will hold enormous promise for replacing plastics made from petrochemicals.

Increased Thermostability of an Engineered Flavin-Containing Monooxygenase to Remediate Trimethylamine in Fish Protein Hydrolysates.

Protein hydrolysates made from marine by-products are very nutritious but frequently contain trimethylamine (TMA), which has an unattractive fish-like smell. Bacterial trimethylamine monooxygenases can oxidize TMA into the odorless trimethylamine N-oxide (TMAO) and have been shown to reduce TMA levels in a salmon protein hydrolysate. To make the flavin-containing monooxygenase (FMO) Methylophaga aminisulfidivorans trimethylamine monooxygenase (mFMO) more suitable for industrial application, we engineered it using the Protein Repair One-Stop Shop (PROSS) algorithm. All seven mutant variants, containing 8 to 28 mutations, displayed increases in melting temperature of between 4.7°C and 9.0°C. The crystal structure of the most thermostable variant, mFMO_20, revealed the presence of four new stabilizing interhelical salt bridges, each involving a mutated residue. Finally, mFMO_20 significantly outperformed native mFMO in its ability to reduce TMA levels in a salmon protein hydrolysate at industrially relevant temperatures. IMPORTANCE Marine by-products are a high-quality source for peptide ingredients, but the unpleasant fishy odor caused by TMA limits their access to the food market. This problem can be mitigated by enzymatic conversion of TMA into the odorless TMAO. However, enzymes isolated from nature must be adapted to industrial requirements, such as the ability to tolerate high temperatures. This study has demonstrated that mFMO can be engineered to become more thermostable. Moreover, unlike the native enzyme, the best thermostable variant efficiently oxidized TMA in a salmon protein hydrolysate at industrial temperatures. Our results present an important next step toward the application of this novel and highly promising enzyme technology in marine biorefineries.

Updates on Plant-Based Protein Products as an Alternative to Animal Protein: Technology, Properties, and Their Health Benefits.

Plant-based protein products, represented by "plant meat", are gaining more and more popularity as an alternative to animal proteins. In the present review, we aimed to update the current status of research and industrial growth of plant-based protein products, including plant-based meat, plant-based eggs, plant-based dairy products, and plant-based protein emulsion foods. Moreover, the common processing technology of plant-based protein products and its principles, as well as the emerging strategies, are given equal importance. The knowledge gap between the use of plant proteins and animal proteins is also described, such as poor functional properties, insufficient texture, low protein biomass, allergens, and off-flavors, etc. Furthermore, the nutritional and health benefits of plant-based protein products are highlighted. Lately, researchers are committed to exploring novel plant protein resources and high-quality proteins with enhanced properties through the latest scientific and technological interventions, including physical, chemical, enzyme, fermentation, germination, and protein interaction technology.

Development and validation of a liquid chromatography-triple quadrupole mass spectrometry method for the determination of isopeptide ε-(γ-glutamyl) lysine in human urine as biomarker for transglutaminase 2 cross-linked proteins

Determination of the levels of protein cross-linking catalysed by the activity of transglutaminase 2 in various disease states has remained a significant challenge. The ability to quantify the isopeptide ε-(γ-glutamyl) lysine, which can form as a heterogeneous bond within or between proteins has significant analytical and clinical potential as a biomarker in biofluids such as human urine. Increased transglutaminase 2 activity is associated with a number of diseases, such as fibrosis. Previously published methods have been based on classical amino acid analysis, however they require a complex multi-enzyme digestion in order to achieve complete protein digestion, whilst leaving the isopeptide cross link intact. These methods require high levels of enzymes, which contaminate the analysis and alter the dynamics of digestion. The amino acid analysis detection also lacked selectivity, especially where the levels of crosslink are expected to be low relative to the background protein levels. We have systematically addressed these challenges, by optimising the precipitation of the protein in urine, the use of innovative immobilised enzyme technology, which allows for efficient digestion without enzyme contamination and LC-MS/MS detection based on multiple reaction monitoring. This method was validated for its analytical performance characteristics, showing the method has a sensitivity of 0.1 ng/mL of ε-(γ-glutamyl) lysine in human urine with precision of less than 20% CV, and is selective as no interferences were observed that may adversely affect the analysis. As such this approach represents a significant advance in the ability to detect and quantify ε-(γ-glutamyl) lysine.

Microbial xylanase aided biobleaching effect on multiple components of lignocelluloses biomass based pulp and paper: a review

Abstract Due to discharge of hazardous organochlorine compounds and absorbable organic halogen compounds in the effluent, the pulp and paper industries are trying to alter the bleaching process to limit the use of chlorine compounds and comply with regulatory, environmental, and market demands. With progress in biotechnology, enzyme technologies can effectively pre-treat lignocellulosic biomass in the pulp and paper making process. Usually, these enzymatic processes reduce the environmental impact of traditional pulp and paper-making processes, lower the overall production cost, and enhance product quality. Microbial xylanases are the potential bio-bleaching candidate due to their renewable, mild operating, highly specific, and eco-friendly nature. Xylanase enhances the efficacy of the bleaching process by breaking the β-1, 4-glycosidic backbone of the re-precipitated xylan network and removing the trapped lignin from the pulp fibers. Xylanolytic action positively influences the kappa number, hexenuronic acid, chromophore compounds release, pulp crystallinity, morphology and many other attributes of pulp. The present review comprehensively highlights the microbial xylanolytic system, its mechanism, and its application in pulp bioleaching. With the recent development, the paper delineates the xylanase-aided bleaching effects on pulp, paper, and effluent attributes aimed to reduce bleaching chemical use, AOX formation, and energy use in the pulp refining process.

Sustainable Refining of Vegetable Oil Made Easy with a Designer Phospholipase C Enzyme

The increasing demand pressures the vegetable oil industry to develop novel refining methods. Degumming with type C phospholipases (PLCs) is a green technology and provides extra oil. However, natural PLCs are not active under the harsh conditions used in oil refining plants, requiring additional unit operations. These upfront capital expenditures and the associated operational costs hinder the adoption of this method. Here, we present a process based on ChPLC, a synthetic PLC obtained by consensus sequence design, possessing superior thermal stability and catalytic properties. Using ChPLC, crude soybean oil degumming was completed at 80 °C in 30 min, the temperature and residence time imposed by the design of existing oil refining plants. Remarkably, an extra yield of oil of 2% was obtained using 60% of the dose recommended for PLCs marketed today, saving upfront investments and reducing the operational cost of degumming. A techno-economic analysis indicates that, for medium size plants, ChPLC reduces the overall cost of soybean oil enzymatic degumming by 58%. The process presented here facilitates the implementation of enzymatic technologies to oil producers, regardless of their processing capacity, bringing potential annual benefits in the billion-dollar range for the global economy.

The current situation of fast fashion industry and how to reduce the waste

Since entering the 21st century, the development of fast fashion has faced a number of environmental problems. The design of circular economy is the best way to deal with fast fashion pollution, while the existing recycling system, traditional waste disposal methods are inefficiencies and are no longer enough to deal with the pollution caused by today's fast fashion industry. So this paper discusses some cutting-edge technologies to meet the development of circular fashion and achieve the approaches for sustainable development of fashion industry. After a specific analysis of the pollution of the fast fashion industry to the climate, water and the waste caused, this paper introduces the infrared technology to accelerate the sorting of clothing raw materials in the waste, enzymatic technology to process and degrade the raw materials, and the use of new sustainable materials in three steps to obtain an advanced technology support, sustainable fashion circulation system. In the future, this improved fast fashion circulation system still needs more experiments to be tested, also the government and relevant departments need to formulate relevant policies to support the development of this system. On the other side, the fast fashion industry's pollution of the environment, especially water bodies, and its treatment methods need to be studied.

Exploring consumer behaviour in automatic dishwashing: a quantitative investigation of appliance usage in six European countries

Abstract Automatic dishwashing has been optimised in manifold ways during the last decades: new dishwashing devices (e.g. optimised for best class in energy labelling) and innovative dishwashing detergents (e.g. with advanced enzyme technologies). However, the usage of the automatic dishwasher in consumers’ home may not be adequate to gain all the benefits from these developments. Little is known about the actual consumer behaviour with automatic dishwashing. This was tried to solve by performing a survey on the consumer behaviour on automatic dishwashing in Germany, Italy, Spain, Poland, Hungary and Turkey covering large parts of Europe. The results show that the ‘eco’-programme is getting more importance in programme selection. However, feedback on the soil level of the dish items put into this programme and the observed duration of the programme show that the potential of the ‘eco’-programme is not fully utilised by consumers. Besides this, the survey delivers relevant details on differences which may help to understand the needs and wishes of consumers in those countries.

Mengintegrasikan Eco Print dan Eco Enzim: Produk Ramah Lingkungan Multi Fungsi di Kampung Delik Sari, Semarang

The textile and agriculture industries are sectors that have a large impact on the environment. Chemicals used in the printing and dyeing processes of cloth and in fertilization can contaminate water and soil, and affect human health. Therefore, the emergence of eco print technology and eco enzymes is an attractive alternative to reduce this negative impact. This community service aims to study the potential use of eco print and eco enzymes in producing multi-functional environmentally friendly products in Delik Sari Village, Semarang. The research method used is training by presenting resource persons in accordance with the fields: eco print and eco enzymes Meanwhile, making eco prints aims to increase better product results and more diverse product diversification. Eco-enzymes produced by bacteria and fungi are used as basic ingredients for making environmentally friendly soaps and household cleaners. The results of community service show that the use of eco print and eco enzyme technology can produce quality fabric products with attractive and durable colors. In addition, the waste products from the eco print and eco enzyme processes can be used as organic fertilizer which is useful for agriculture in Delik Sari Village. Thus, eco print and eco enzyme technologies have great potential to produce multi-functional environmentally friendly products that can improve the welfare of the people of Kampung Delik Sari, Gunung Pati sub-district, Semarang City.

The Recent Advances in the Utility of Microbial Lipases: A Review

Lipases are versatile biocatalysts and are used in different bioconversion reactions. Microbial lipases are currently attracting a great amount of attention due to the rapid advancement of enzyme technology and its practical application in a variety of industrial processes. The current review provides updated information on the different sources of microbial lipases, such as fungi, bacteria, and yeast, their classical and modern purification techniques, including precipitation and chromatographic separation, the immunopurification technique, the reversed micellar system, aqueous two-phase system (ATPS), aqueous two-phase flotation (ATPF), and the use of microbial lipases in different industries, e.g., the food, textile, leather, cosmetics, paper, and detergent industries. Furthermore, the article provides a critical analysis of lipase-producing microbes, distinguished from the previously published reviews, and illustrates the use of lipases in biosensors, biodiesel production, and tea processing, and their role in bioremediation and racemization.

Abstract TMP45: Nanobiotechnology-based, Ultra-rapid Test For Brain Injuries To Accelerate Differential Diagnosis Of Stroke From Mimics

Introduction: Stroke is the 5th leading cause of death, and a leading cause of long-term disability in the US. Thus, there is a need for a rapid biomarker-based screen that enables an objective and timely diagnosis and better patient outcome; however, the lack of such a technology delays diagnosis and treatment, increases misdiagnosis, and leads to the overuse of thrombolysis in patients with stroke mimics. Methods: Here we present pilot data of a nanobiotechnology based test platform, in which enzyme-functionalized nanoparticles (TET, Tethered Enzyme Technology) are used for ultra-rapid biomarker detection. As proof of concept, we used TET to quantify the enzymatic activity of a widely studied brain injury biomarker, neuron-specific enolase (NSE), in a trial performed at a regional stroke center. Results: Plasma from 36 suspected stroke and 17 asymptomatic subjects (Total N=53) was tested to determine levels of the novel biomarker NSE catalytic activity (NSE-A) versus the conventional NSE protein (NSE-P). Based on clinical diagnoses, our data demonstrate a significant increase in the levels of NSE-A in subjects suffering from injury to neurons (BI, Brain Injury) compared to those with negative diagnoses (Neg, stroke mimics). Moreover, we show that NSE-A provides a considerable diagnostic advantage over the NIH Stroke Scale or NSE-P (Figure 1A-C) in both clinical utility and speed. In diagnosis of stroke mimics (including TIAs and Neg) versus BI, NSE-A showed significantly better performance than NIHSS or NSE-P, as shown by ROC and AUC analyses (Figure 1D). Conclusions: TET-based detection of NSE-A can rapidly differentiate patients suffering a neuronal injury, including stroke, from those presenting with stroke mimics. Upon further development of a point-of-care test for NSE-A and other biomarkers, TET could be an asset to ongoing efforts to streamline stroke patient care, reduce door to needle time, and decrease overall brain injury and long-term disability.

Decellularized matrix for repairing intervertebral disc degeneration: Fabrication methods, applications and animal models.

Intervertebral disc degeneration (IDD)-induced low back pain significantly influences the quality of life, placing a burden on public health systems worldwide. Currently available therapeutic strategies, such as conservative or operative treatment, cannot effectively restore intervertebral disc (IVD) function. Decellularized matrix (DCM) is a tissue-engineered biomaterial fabricated using physical, chemical, and enzymatic technologies to eliminate cells and antigens. By contrast, the extracellular matrix (ECM), including collagen and glycosaminoglycans, which are well retained, have been extensively studied in IVD regeneration. DCM inherits the native architecture and specific-differentiation induction ability of IVD and has demonstrated effectiveness in IVD regeneration in vitro and in vivo. Moreover, significant improvements have been achieved in the preparation process, mechanistic insights, and application of DCM for IDD repair. Herein, we comprehensively summarize and provide an overview of the roles and applications of DCM for IDD repair based on the existing evidence to shed a novel light on the clinical treatment of IDD.