Displaying publications 1 - 20 of 66 in total

Abstract:
Sort:
  1. An integrated overview of bacterial carboxylesterase: Structure, function and biocatalytic applications
    Johan UUM, Rahman RNZRA, Kamarudin NHA, Ali MSM
    Colloids Surf B Biointerfaces, 2021 Sep;205:111882.
    PMID: 34087776 DOI: 10.1016/j.colsurfb.2021.111882
    Carboxylesterases (CEs) are members of prominent esterase, and as their name imply, they catalyze the cleavage of ester linkages. By far, a considerable number of novel CEs have been identified to investigate their exquisite physiological and biochemical properties. They are abundant enzymes in nature, widely distributed in relatively broad temperature range and in various sources; both macroorganisms and microorganisms. Given the importance of these enzymes in broad industries, interest in the study of their mechanisms and structural-based engineering are greatly increasing. This review presents the current state of knowledge and understanding about the structure and functions of this ester-metabolizing enzyme, primarily from bacterial sources. In addition, the potential biotechnological applications of bacterial CEs are also encompassed. This review will be useful in understanding the molecular basis and structural protein of bacterial CEs that are significant for the advancement of enzymology field in industries.
    Matched MeSH terms: Biocatalysis
  2. Enhancing plastic biodegradation process: strategies and opportunities
    Crystal Thew XE, Lo SC, Ramanan RN, Tey BT, Huy ND, Chien Wei O
    Crit Rev Biotechnol, 2024 May;44(3):477-494.
    PMID: 36788704 DOI: 10.1080/07388551.2023.2170861
    Plastic biodegradation has emerged as a sustainable approach and green alternative in handling the ever-increasing accumulation of plastic wastes in the environment. The complete biodegradation of polyethylene terephthalate is one of the most recent breakthroughs in the field of plastic biodegradation. Despite the success, the effective and complete biodegradation of a wide variety of plastics is still far from the practical implementation, and an on-going effort has been mainly devoted to the exploration of novel microorganisms and enzymes for plastic biodegradation. However, alternative strategies which enhance the existing biodegradation process should not be neglected in the continuous advancement of this field. Thus, this review highlights various strategies which have shown to improve the biodegradation of plastics, which include the pretreatment of plastics using UV irradiation, thermal, or chemical treatments to increase the susceptibility of plastics toward microbial action. Alternative pretreatment strategies are also suggested and compared with the existing techniques. Besides, the effects of additives such as pro-oxidants, natural polymers, and surfactants on plastic biodegradation are discussed. In addition, considerations governing the biodegradation performance, such as the formulation of biodegradation medium, cell-free biocatalysis, and physico-chemical properties of plastics, are addressed. Lastly, the challenges and future prospects for the advancement of plastic biodegradation are also highlighted.
    Matched MeSH terms: Biocatalysis
  3. Efficient and easible biocatalysts: Strategies for enzyme improvement. A review
    Albayati SH, Nezhad NG, Taki AG, Rahman RNZRA
    Int J Biol Macromol, 2024 Sep;276(Pt 2):133978.
    PMID: 39038570 DOI: 10.1016/j.ijbiomac.2024.133978
    Owing to the environmental friendliness and vast advantages that enzymes offer in the biotechnology and industry fields, biocatalysts are a prolific investigation field. However, the low catalytic activity, stability, and specific selectivity of the enzyme limit the range of the reaction enzymes involved in. A comprehensive understanding of the protein structure and dynamics in terms of molecular details enables us to tackle these limitations effectively and enhance the catalytic activity by enzyme engineering or modifying the supports and solvents. Along with different strategies including computational, enzyme engineering based on DNA recombination, enzyme immobilization, additives, chemical modification, and physicochemical modification approaches can be promising for the wide spread of industrial enzyme usage. This is attributed to the successful application of biocatalysts in industrial and synthetic processes requires a system that exhibits stability, activity, and reusability in a continuous flow process, thereby reducing the production cost. The main goal of this review is to display relevant approaches for improving enzyme characteristics to overcome their industrial application.
    Matched MeSH terms: Biocatalysis*
  4. Catalytically active inclusion bodies as a potential tool for biotechnology
    Bello MN, Sabri S, Mohd Yahaya N, Mohd Shariff F, Mohamad Ali MS
    Biotechnol Appl Biochem, 2024 Dec;71(6):1235-1242.
    PMID: 38863240 DOI: 10.1002/bab.2624
    The initial assumption that viewed inclusion bodies as a hindrance to the efficient production of protein is no longer held due to the emergence of catalytically active inclusion bodies (CatIBs). Recent studies revealed their potential to be used in free form or immobilized as biocatalysts. The curiosity to acquire suitable catalysts has remained the measure of concern for researchers and industrialists. Numerous processes and production in various sectors of food industries, petroleum, pharmaceutical, cosmetics, and many others are still searching for a robust catalyst with outstanding features such as recyclability, resistance to pH, as well as temperature. CatIBs are forms of inclusion bodies that possess catalytic activity, which can improve catalysis efficiency, stability, and recyclability. One of the advantages of CatIBs is their potential to be used as catalysts for numerous bioprocesses when generated by an enzyme. These aggregates can efficiently be used as a replacement for traditional enzyme immobilization. This review tends to focus on the possibility of its application in various processes. The novelty of this review is that it considered the production of CatIBs both from artificial and natural perspectives, as well as how to improve it. Inclusion bodies' immobilization may provide an efficient alternative in the area of biocatalysis, and hence it will improve industrial sectors and substantially provide a means of achieving excellent performance in the near future.
    Matched MeSH terms: Biocatalysis*
  5. Fulltext Stability study of an exothermic biocatalytic reaction and its application in bioprocess systems
    Mohd. Radzi, M.R., Uzir, M.H.
    Pertanika Journal of Science & Technology, 2009;17(1):-.
    MyJurnal
    Biocatalytic reaction is a type of reaction which uses enzyme or whole-cell as a (bio)-catalyst to achieve a desired conversion, under controlled conditions in a bioreactor. Temperature produces opposed effects on enzyme activity and stability, and is therefore a key variable in any biocatalytic processes. An exothermic biocatalytic reaction, in a continuous-stirred-tank reactor (CSTR), was analyzed where dynamic equations (non-linear differential equations) could be derived from the Michaelis-Menten and Arrhenius equations, by performing mass and energy balances on the reactor. In this work, the effects of the different parameters such as dilution rate, proportional control constant and dimensionless total enzyme concentration, on the stability of the system, were studied. The stability of the reaction could be analyzed, based on the ODE (ordinary differential equation), solved using the numerical technique in MATLAB® and the analytical investigation using Mathematica.® The numerical analysis can be carried out by considering the hase-plane behaviour and bifurcation diagrams of the dynamic equations, while the analytical analysis using Mathematica® can be undertaken by evaluating the eigenvalues of the system. In order to model the operational stability of biocatalysts, modulation factors need to be considered so that a proper design of bioreactors can be done. Temperature, as a key variable in such bioprocess systems, can be conveniently optimized through the use of appropriate models.
    Matched MeSH terms: Biocatalysis
  6. Fulltext Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications
    Sharma T, Xia C, Sharma A, Raizada P, Singh P, Sharma S, et al.
    Bioengineered, 2022 Apr;13(4):10518-10539.
    PMID: 35443858 DOI: 10.1080/21655979.2022.2062526
    Enzymes of commercial importance, such as lipase, amylase, laccase, phytase, carbonic anhydrase, pectinase, maltase, glucose oxidase etc., show multifunctional features and have been extensively used in several fields including fine chemicals, environmental, pharmaceutical, cosmetics, energy, food industry, agriculture and nutraceutical etc. The deployment of biocatalyst in harsh industrial conditions has some limitations, such as poor stability. These drawbacks can be overcome by immobilizing the enzyme in order to boost the operational stability, catalytic activity along with facilitating the reuse of biocatalyst. Nowadays, functionalized polymers and composites have gained increasing attention as an innovative material for immobilizing the industrially important enzyme. The different types of polymeric materials and composites are pectin, agarose, cellulose, nanofibers, gelatin, and chitosan. The functionalization of these materials enhances the loading capacity of the enzyme by providing more functional groups to the polymeric material and hence enhancing the enzyme immobilization efficiency. However, appropriate coordination among the functionalized polymeric materials and enzymes of interest plays an important role in producing emerging biocatalysts with improved properties. The optimal coordination at a biological, physical, and chemical level is requisite to develop an industrial biocatalyst. Bio-catalysis has become vital aspect in pharmaceutical and chemical industries for synthesis of value-added chemicals. The present review describes the current advances in enzyme immobilization on functionalized polymers and composites. Furthermore, the applications of immobilized enzymes in various sectors including bioremediation, biosensor and biodiesel are also discussed.
    Matched MeSH terms: Biocatalysis
  7. Fulltext A dual-function Savinase-catalyzed strategy for enhanced bioactive protein hydrolysate production from Nannochloropsis oculata for personal care and cosmetic applications
    Susanto S, Ng WZ, Liow MY, Sahadevan S, Chan ES, Borhan N, et al.
    Int J Biol Macromol, 2026 Nov;381(Pt 2):154294.
    PMID: 42680025 DOI: 10.1016/j.ijbiomac.2026.154294
    Microalgae are a sustainable source of bioactive proteins for personal care and cosmetic applications. Conventional alkaline extraction can achieve high protein recovery but relies on harsh chemical conditions that often compromise protein integrity, reduce bioactivity, and raise environmental concerns. Moreover, the extracted proteins often require additional enzymatic hydrolysis to enhance their functionality, thus increasing process complexity. This study proposes a dual-function Savinase-assisted in situ extraction strategy for the simultaneous extraction and functionalization of protein from Nannochloropsis oculata (N. oculata). Process optimization using improvement in protein extraction yield (IPEY) as the performance indicator identified optimal conditions of pH 7, 50 °C, 0.5 wt% Savinase and 2 h hydrolysis, under which a maximum IPEY of 85.1% was achieved. Fluorescence spectroscopy and zeta potential measurements confirmed that Savinase remained structurally stable under the optimized conditions while promoting protein solubilization. The resulting protein hydrolysates exhibited enhanced functional properties, with ABTS•+ radical scavenging activity reaching 83.3% at 5 mg/mL, representing a 56.9% increase compared with the non-enzymatic control. In addition, UV absorption analysis revealed a critical wavelength (λc) of 383.6 nm, indicating broad-spectrum photoprotective potential. Overall, the proposed one-step Savinase-assisted process provides a mild, sustainable, and effective strategy for producing bioactive microalgal protein hydrolysates with strong potential as natural ingredients in skin-protective cosmetic formulations.
    Matched MeSH terms: Biocatalysis
  8. Quantum mechanical tunnelling through the catalytic effects of A2451 ribosomal residue during a stepwise peptide bond formation
    Monajemi H, Md Zain S, Ishida T, Wan Abdullah WAT
    Biochem. Cell Biol., 2019 08;97(4):497-503.
    PMID: 30444637 DOI: 10.1139/bcb-2018-0220
    The search for the mechanism of ribosomal peptide bond formation is still ongoing. Even though the actual mechanism of peptide bod formation is still unknown, the dominance of proton transfer in this reaction is known for certain. Therefore, it is vital to take the quantum mechanical effects on proton transfer reaction into consideration; the effects of which were neglected in all previous studies. In this study, we have taken such effects into consideration using a semi-classical approach to the overall reaction mechanism. The M06-2X density functional with the 6-31++G(d,p) basis set was used to calculate the energies of the critical points on the potential energy surface of the reaction mechanism, which are then used in transition state theory to calculate the classical reaction rate. The tunnelling contribution is then added to the classical part by calculating the transmission permeability and tunnelling constant of the reaction barrier, using the numerical integration over the Boltzmann distribution for the symmetrical Eckart potential. The results of this study, which accounts for quantum effects, indicates that the A2451 ribosomal residue induces proton tunnelling in a stepwise peptide bond formation.
    Matched MeSH terms: Biocatalysis*
  9. Laccase enzymes: purification, structure to catalysis and tailoring
    Moin SF, Omar MN
    Protein Pept Lett, 2014;21(8):707-13.
    PMID: 23855667
    Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen molecule to produce water. These enzymes are glycosylated proteins and have been isolated and purified from fungi, bacteria, plant, insects and lichens. The variety of commercial and industrial application of laccases has attracted much attention towards the research addressing different aspects of the protein characterization, production and fit for purpose molecule. Here we briefly discuss the purification, catalytic mechanism in light of available understanding of structure-function relationship and the tailoring side of the protein, which has been the subject of recent research. Purification strategy of laccases is a method of choice and is facilitated by increased production of the enzyme. The structure-function relationship has given insights to unfold the catalytic mechanism. Site directed mutagenesis and other modification at C-terminal end or surrounding environment of copper centres have shown promising results to fit for purpose aspect, with a lot remains to be explored in glycosylation status and its alteration.
    Matched MeSH terms: Biocatalysis*
  10. Enzymatic preparation of diacylglycerols: lipase screening, immobilization, characterization and glycerolysis performance
    Xie R, Peng X, Lee YY, Xie P, Tan CP, Wang Y, et al.
    J Sci Food Agric, 2025 Jan 30;105(2):816-828.
    PMID: 39258418 DOI: 10.1002/jsfa.13872
    BACKGROUNDS: Glycerolysis, with its advantages of readily available raw materials, simple operation, and mild reaction conditions, is a primary method for producing diacylglycerol (DAG). However, enzymatic glycerolysis faces challenges such as high enzyme costs, low reuse efficiency, and poor stability. The study aims to develop a cost-effective immobilized enzyme by covalently binding lipase to pre-activated carriers through the selection of suitable lipases, carriers, and activating agents. The optimization is intended to improve the glycerolysis reaction for efficient DAG production.

    RESULTS: Lipase CN-TL (from Thermomyces lanuginosus) was selected through glycerolysis reaction and molecular docking to catalyze the glycerolysis reaction. Optimizing the immobilization method by covalently binding CN-TL to poly(ethylene glycol) diglycidyl ether (PEGDGE)-preactivated resin LX-201A resulted in the preparation of the immobilized enzyme TL-PEGDGE-LX. The immobilized enzyme retained over 90% of its initial activity after five consecutive reactions, demonstrating excellent reusability. The DAG content in the product remained at 84.8% of its initial level, further highlighting the enzyme's potential for reusability and its promising applications in the food and oil industries.

    CONCLUSIONS: The immobilized lipase TL-PEGDGE-LX, created by covalently immobilizing lipase CN-TL on PEGDGE-preactivated carriers, demonstrated broad applicability and excellent reusability. This approach offers an economical and convenient immobilization strategy for the enzymatic glycerolysis production of DAG. © 2024 Society of Chemical Industry.

    Matched MeSH terms: Biocatalysis*
  11. Lipase-catalyzed esterification for efficient acylglycerols synthesis in a solvent-free system: Process optimization, mass transfer insights and kinetic modeling
    Zou S, Zhang Z, Lee YY, Ai H, Zhang Y, Wang Y
    Food Chem, 2025 May 15;474:143151.
    PMID: 39891972 DOI: 10.1016/j.foodchem.2025.143151
    Acylglycerols are widely used in the food industry due to their antimicrobial, emulsifying and nutritional properties. This study investigated the key reaction parameters, mass transfer mechanisms, and kinetic features of lipase-catalyzed esterification in a solvent-free system. Taguchi method was further employed to explore the relationship between "reaction parameter - yield composition". The results revealed that the maximum selectivity were achieved fror MAG (57.72 %), DAG (82.67 %) and TAG (79.29 %) under different enzymatic conditions. Fatty acid-to-glycerol molar ratio had the greatest impact on DAG selectivity, contributing 38.08 % of total impact level. Mass transfer analysis showed that external mass transfer limitation could be effectively overcome at stirring speeds above 600 rpm. Kinetic analysis confirmed that the reaction followed the Ping-Pong BiBi mechanism with alcohol and acid inhibition (SSE = 0.000643). This work provided a theoretical basis for developing more efficient and selective catalytic processes, aiding in quality control, reactor design, and industrial scale-up.
    Matched MeSH terms: Biocatalysis*
  12. A hybrid enzymatic zinc-air fuel cell
    Abdul Aziz Ahmad, Raihan Othman, Faridah Yusof, Mohd Firdaus Abdul Wahab
    Sains Malaysiana, 2014;43:459-465.
    A hybrid biofuel cell, a zinc-air cell employing laccase as the oxygen reduction catalyst is investigated. A simple cell design is employed; a membraneless single chamber and a freely suspended laccase in the buffer electrolyte. The cell is characterised based on its open-circuit voltage, power density profile and galvanostatic discharge at 0.5 mA. The activity of laccase as an oxidoreductase is substantiated from the cell discharge profiles. The use of air electrode in the cell design enhanced the energy output by 14%. The zinc-air biofuel cell registered an open-circuit voltage of 1.2 V and is capable to deliver a maximum power density of 1.1 mWcm-2 at 0.4 V. Despite its simple design features, the power output is comparable to that of biocatalytic cell utilising a much more complex system design.
    Matched MeSH terms: Biocatalysis
  13. Biocatalytic remediation of pharmaceutically active micropollutants for environmental sustainability
    Bilal M, Lam SS, Iqbal HMN
    Environ Pollut, 2022 Jan 15;293:118582.
    PMID: 34856243 DOI: 10.1016/j.envpol.2021.118582
    The discharge of an alarming number of recalcitrant pollutants from various industrial activities presents a serious threat to environmental sustainability and ecological integrity. Bioremediation has gained immense interest around the world due to its environmentally friendly and cost-effective nature. In contrast to physical and chemical methods, the use of microbial enzymes, particularly immobilized biocatalysts, has been demonstrated as a versatile approach for the sustainable mitigation of environmental pollution. Considerable attention is now devoted to developing novel enzyme engineering approaches and state-of-the-art bioreactor design for ameliorating the overall bio-catalysis and biodegradation performance of enzymes. This review discusses the contemporary and state of the art technical and scientific progress regarding applying oxidoreductase enzyme-based biocatalytic systems to remediate a vast number of pharmaceutically active compounds from water and wastewater bodies. A comprehensive insight into enzyme immobilization, the role of mediators, bioreactors designing, and transformation products of pharmaceuticals and their associated toxicity is provided. Additional studies are necessary to elucidate enzymatic degradation mechanisms, monitor the toxicity levels of the resulting degraded metabolites and optimize the entire bio-treatment strategy for technical and economical affordability.
    Matched MeSH terms: Biocatalysis
  14. Recent advances in the biocatalytic mitigation of emerging pollutants: A comprehensive review
    Ekeoma BC, Ekeoma LN, Yusuf M, Haruna A, Ikeogu CK, Merican ZMA, et al.
    J Biotechnol, 2023 Jun 10;369:14-34.
    PMID: 37172936 DOI: 10.1016/j.jbiotec.2023.05.003
    The issue of environmental pollution has been worsened by the emergence of new contaminants whose morphology is yet to be fully understood . Several techniques have been adopted to mitigate the pollution effects of these emerging contaminants, and bioremediation involving plants, microbes, or enzymes has stood out as a cost-effective and eco-friendly approach. Enzyme-mediated bioremediation is a very promising technology as it exhibits better pollutant degradation activity and generates less waste. However, this technology is subject to challenges like temperature, pH, and storage stability, in addition to recycling difficulty as it is arduous to isolate them from the reaction media. To address these challenges, the immobilization of enzymes has been successfully applied to ameliorate the activity, stability, and reusability of enzymes. Although this has significantly increased the uses of enzymes over a wide range of environmental conditions and facilitated the use of smaller bioreactors thereby saving cost, it still comes with additional costs for carriers and immobilization. Additionally, the existing immobilization methods have their individual limitations. This review provides state-of-the-art information to readers focusing on bioremediation using enzymes. Different parameters such as: the sustainability of biocatalysts, the ecotoxicological evaluation of transformation contaminants, and enzyme groups used were reviewed. The efficacy of free and immobilized enzymes, materials and methods for immobilization, bioreactors used, challenges to large-scale implementation, and future research needs were thoroughly discussed.
    Matched MeSH terms: Biocatalysis
  15. Enhancing PET biocatalytic degradation using a surface-active metabolite formulation derived from Trichoderma asperellum PBW1
    Xuyang W, Lu Y, Jiajun J, Kun TZ, Zhuo T, Zhiwen X, et al.
    J Hazard Mater, 2026 Oct 01;517:143531.
    PMID: 42715668 DOI: 10.1016/j.jhazmat.2026.143531
    Polyethylene terephthalate (PET) pollution necessitates biotechnological strategies that enhance interaction between the hydrophobic surfaces of PET and microbial biocatalysts. In this study, we developed PBW1-SAMF, an operationally defined autoclaved surface-active metabolite formulation derived from Trichoderma asperellum PBW1, which was isolated from plastic-contaminated mangrove sediments in Malaysia. The analyses conducted using liquid chromatography-mass spectrometry (LC-MS), Fourier-transform infrared spectroscopy (FTIR), and nuclear magnetic resonance (NMR) spectroscopy suggested that PBW1-SAMF is a lipid-rich, multicomponent formulation containing surface-active and bioemulsifier-like constituents. However, blank-overlapping LC-MS features were excluded from PBW1-specific interpretation. PBW1-SAMF was evaluated in two PET biocatalytic systems: a PET-degrading yeast-like fungus, Geotrichum sp. ETG, and a recombinant Escherichia coli whole-cell biocatalyst expressing Ester7845. In the fungal system, PBW1-SAMF increased terephthalic acid (TPA) release by approximately 3.8-fold in comparison with the ETG-only control. In the recombinant bacterial system, PBW1-SAMF increased blank-corrected TPA release by approximately 80-fold in comparison with the whole-cell control, although the absolute unit-corrected apparent PET-equivalent conversion remained low. PBW1-SAMF also showed stronger enhancement than the tested commercial biosurfactant treatments under the present recombinant whole-cell reaction conditions. Contact angle, CFU enumeration, extracellular OD260/OD280 leakage assessment, and inhibition-zone assays supported improved PET wettability and whole-cell compatibility. In summary, PBW1-SAMF is a multicomponent formulation-level enhancer derived from fermentation, which increases soluble PET-derived product release. However, further formulation standardisation, mechanistic validation, and complete mass-balance analysis are required to further investigate its efficacy.
    Matched MeSH terms: Biocatalysis
  16. Catalytic pyrolysis of Chlorella vulgaris: Kinetic and thermodynamic analysis
    Fong MJB, Loy ACM, Chin BLF, Lam MK, Yusup S, Jawad ZA
    Bioresour Technol, 2019 Oct;289:121689.
    PMID: 31252316 DOI: 10.1016/j.biortech.2019.121689
    In the present study, catalytic pyrolysis of Chlorella vulgaris biomass was conducted to analyse the kinetic and thermodynamic performances through thermogravimetric approach. HZSM-5 zeolite, limestone (LS), bifunctional HZSM-5/LS were used as catalysts and the experiments were heated from 50 to 900 °C at heating rates of 10-100 °C/min. Iso-conversional model-free methods such as Flynn-Wall-Ozawa (FWO), Kissinger-Akahira-Sunose (KAS), Starink's, and Vyazovkin (V) were employed to evaluate the kinetic parameters meanwhile the thermodynamic parameters were determined by using FWO and KAS methods. The calculated EA values of non-catalytic and catalytic pyrolysis of HZSM-5 zeolite, LS, and bifunctional HZSM-5/LS were determined to be in the range of 156.16-158.10 kJ/mol, 145.26-147.84 kJ/mol, 138.81-142.06 kJ/mol, and 133.26 kJ/mol respectively. The results have shown that catalytic pyrolysis with the presence of bifunctional HZSM-5/LS resulted to a lower average EA and ΔH compared to HZSM-5, and LS which indicated less energy requirement in the process.
    Matched MeSH terms: Biocatalysis
  17. Effect of Purification Methods on the Physicochemical and Thermodynamic Properties and Crystallization Kinetics of Medium-Chain, Medium-Long-Chain, and Long-Chain Diacylglycerols
    Wang S, Lee WJ, Wang Y, Tan CP, Lai OM, Wang Y
    J Agric Food Chem, 2020 Aug 05;68(31):8391-8403.
    PMID: 32511921 DOI: 10.1021/acs.jafc.0c01346
    Medium-chain diacylglycerol (MCD), medium-long-chain diacylglycerol (MLCD), and long-chain diacylglycerol (LCD) were prepared through enzymatic esterification using different conditions at temperatures of 55-70 °C and reaction times of 1.5-5 h and in the presence of 5-6% Novozym 435. Subsequently, purification was performed using three different techniques, namely, molecular distillation (MD), deodorization (DO), and silica gel column chromatography (SGCC). Variations in terms of the physicochemical and thermodynamic properties, crystallization properties, and kinetics of the diacylglycerols (DAGs) before and after purification were determined. Irrespective of the DAG chain lengths, SGCC was able to produce samples with high DAG purity (96-99 wt %), followed by MD (58-79 wt %) and DO (39-59 wt %). A higher 1,3-DAG/1,2-DAG ratio was recorded for all samples, with the highest ratio recorded for SGCC purified samples. Regardless of the purification techniques used, the solid fat content (SFC) profiles of crude samples with steep curves were altered post-purification, showing a gradual increment in SFC along with increasing temperature. Modification of the Avrami constant and coefficient suggested the modification of the crystal growth mechanism post-purification. Crystallization and melting temperatures of products with a higher DAG purity were shifted to a higher temperature region. Variations were also reflected in terms of the crystal polymorphism, whereby the α and β' crystals transitioned into the more stable β form in purified samples accompanied by modification in the microstructures and crystal sizes. However, there was insignificant change in the morphology of MLCD crystal after purification, except for the decrease in crystal sizes. In conclusion, synthesis of MCD, MLCD, and LCD comprising different DAG purities had distinctive SFC profiles, thermodynamic properties, crystallization kinetics, and crystal morphologies, which can be further incorporated into the preparation of a variety of fat products to obtain end products with desired characteristics.
    Matched MeSH terms: Biocatalysis
  18. Fulltext Recent advancements in enzyme-incorporated nanomaterials: Synthesis, mechanistic formation, and applications
    Anboo S, Lau SY, Kansedo J, Yap PS, Hadibarata T, Jeevanandam J, et al.
    Biotechnol Bioeng, 2022 Oct;119(10):2609-2638.
    PMID: 35851660 DOI: 10.1002/bit.28185
    Over the past decade, nanotechnology has been developed and employed across various entities. Among the numerous nanostructured material types, enzyme-incorporated nanomaterials have shown great potential in various fields, as an alternative to biologically derived as well as synthetically developed hybrid structures. The mechanism of incorporating enzyme onto a nanostructure depends on several factors including the method of immobilization, type of nanomaterial, as well as operational and environmental conditions. The prospects of enzyme-incorporated nanomaterials have shown promising results across various applications, such as biocatalysts, biosensors, drug therapy, and wastewater treatment. This is due to their excellent ability to exhibit chemical and physical properties such as high surface-to-volume ratio, recovery and/or reusability rates, sensitivity, response scale, and stable catalytic activity across wide operating conditions. In this review, the evolution of enzyme-incorporated nanomaterials along with their impact on our society due to its state-of-the-art properties, and its significance across different industrial applications are discussed. In addition, the weakness and future prospects of enzyme-incorporated nanomaterials were also discussed to guide scientists for futuristic research and development in this field.
    Matched MeSH terms: Biocatalysis
  19. Fulltext Unveiling the role of mechanical process intensifications and chemical additives in boosting lipase-catalyzed hydrolysis of vegetable oil for fatty acid production: A comprehensive review
    Ng WZ, Chan ES, Gourich W, Adiiba SH, Liow MY, Ooi CW, et al.
    Int J Biol Macromol, 2025 Jan;284(Pt 1):138144.
    PMID: 39613062 DOI: 10.1016/j.ijbiomac.2024.138144
    The enzymatic production of fatty acids from vegetable oils is becoming a preferred method due to its mild conditions, simplicity, and scalability. This review analyzes studies on enzymatic hydrolysis, exploring various feedstocks, lipases, reaction conditions, and conversion yields. However, a key limitation is the longer reaction time compared to conventional methods. This limitation is primarily due to the immiscibility of triacylglycerols (TAGs) with water at low temperatures and pressures, as well as the lower activity of enzymes compared to chemical catalysts. To overcome these issues, chemical additives are identified as the most effective process intensification strategy. They are easy to implement, cause less damage to lipases, and are more efficient than mechanical methods. The impact of various chemical additives was thoroughly examined for potential improvements in the enzymatic hydrolysis of vegetable oils. A synergistic combination of chemical additives comprising ionic liquids (ILs) and polyols, along with ultrasound, as well as the consideration of immobilization techniques were explored. Overall, this review highlights the potential of chemical additives and their synergistic feasibility in enhancing the enzymatic performance of lipase-catalyzed hydrolysis reactions.
    Matched MeSH terms: Biocatalysis
  20. Structure-Guided Engineering of Cu/Zn Superoxide Dismutase for Enhanced Catalytic Efficiency and Thermostability
    Al-Adeeb A, Muhammad Aqeel S, Al-Jaberi HS, Gu Q, Al-Ansi W, Al-Maqtari QA, et al.
    J Agric Food Chem, 2026 Oct 28;74(42):33165-33183.
    PMID: 42949349 DOI: 10.1021/acs.jafc.6c10478
    Cu/Zn superoxide dismutase (Cu/Zn-SOD) is a key antioxidant enzyme that catalyzes superoxide radical dismutation. Here, an integrated computational-assisted, structure-guided engineering strategy was applied to improve Cu/Zn-SOD catalytic performance. Gln22 and Glu134 were identified as promising engineering sites, and saturation mutagenesis yielded Q22I and E134 M as the most beneficial single substitutions, with specific activities 1.55- and 2.39-fold higher than wild type (WT), respectively. Combining both substitutions generated M2 (Q22I/E134M), which showed the highest specific activity of 7121.0 U mg-1, corresponding to a 3.43-fold increase over WT. The optimal temperature of Q22I and M2 increased from 40 to 50 °C, and M2 also exhibited enhanced thermostability. Kinetic analysis showed that M2 had a 41.18% lower Km and a 2.95-fold higher Vmax than WT. Molecular docking suggested complementary effects of Q22I and E134 M on structural stability and active-site optimization, supporting improved catalytic performance. These findings provide a basis for engineering efficient, thermostable SODs.
    Matched MeSH terms: Biocatalysis
Related Terms
Filters
Contact Us

Please provide feedback to Administrator (afdal@afpm.org.my)

External Links