Madan Lal Verma
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Madan Lal Verma has a total of 231 co-authors. Here are the top co-authors by number of shared publications:
- Shamsher Singh Kanwar
Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla 171 005, India
10 shared publications - Munish Puri
Bioprocessing Laboratory, Medical Biotechnology, College of Medicine and Public Health, Flinders University, Bedford Park, Adelaide 5042, Australia
8 shared publications - Colin James Barrow
Centre for Sustainable Bioproducts Deakin University Geelong Victoria Australia
7 shared publications - Ghanshyam Singh Chauhan
Department of Chemistry, Himachal Pradesh University, Summer Hill, Shimla, Himachal Pradesh 171005, India
5 shared publications Varsha Rani
Shoolini University
5 shared publications- Bo Wang
School of Behavioural and Health Science, Australian Catholic University, Sydney, NSW 2060, Australia
3 shared publications
Latest Publications
- 2 September 2026
- Published by Springer Nature
- p. 415-438
Nanocarriers Immobilized Enzymes and Their Potential Industrial Applications
- 2 September 2026
- Published by Springer Nature
- p. 415-438
Nanocarriers Immobilized Enzymes and Their Potential Industrial Applications
- Open Access
- 28 June 2026
- Published by MDPI AG in Applied Microbiology
- Vol. 6 (7) , 73
Bioinformatics Tools and Big Data Analytics for Understanding Agricultural Microbial Ecosystems
Microbial diversity and sustainable agriculture are key players for the mutual harmony of the nature/agriculture ecosystem that align with the Sustainable Development Goals (SDGs). However, to harness their best potential, it is necessary to understand the complex interactions between microbial communities and plants. This has become feasible with the intervention of advanced multiomics techniques including genomics, metagenomics, transcriptomics, proteomics, metabolomics, etc. With the advent of next-generation technologies, production of biological data at a cost-effective expense has escalated rapidly. Thus, it is feasible for all researchers to explore these advanced technologies for a better understanding of how to harness the full potential of microbial diversity toward sustainable agriculture. The growth of biological databases, particularly microbial databases, and interphasic tools are bound to the rapid growth of bioinformatics domains. Additionally, bioinformatics provides the direction for better understanding of the interaction of the microbe–plant system. Keeping in view the expansion of escalated biological datasets, the role of big data analytics is vital to understand the interplay of the diverse datasets along with the growing biological databases. The relevant case studies employing big data analytics in sustainable agriculture have been discussed. This will help to make better decisions toward the productivity of sustainable agriculture. This review is an attempt to showcase the recent growth of bioinformatics databases and the role of big data analytics in achieving sustainable agriculture.
- 28 June 2026
- Published by MDPI AG in Applied Microbiology
- Vol. 6 (7) , 73
Open AccessBioinformatics Tools and Big Data Analytics for Understanding Agricultural Microbial Ecosystems
Microbial diversity and sustainable agriculture are key players for the mutual harmony of the nature/agriculture ecosystem that align with the Sustainable Development Goals (SDGs). However, to harness their best potential, it is necessary to understand the complex interactions between microbial communities and plants. This has become feasible with the intervention of advanced multiomics techniques including genomics, metagenomics, transcriptomics, proteomics, metabolomics, etc. With the advent of next-generation technologies, production of biological data at a cost-effective expense has escalated rapidly. Thus, it is feasible for all researchers to explore these advanced technologies for a better understanding of how to harness the full potential of microbial diversity toward sustainable agriculture. The growth of biological databases, particularly microbial databases, and interphasic tools are bound to the rapid growth of bioinformatics domains. Additionally, bioinformatics provides the direction for better understanding of the interaction of the microbe–plant system. Keeping in view the expansion of escalated biological datasets, the role of big data analytics is vital to understand the interplay of the diverse datasets along with the growing biological databases. The relevant case studies employing big data analytics in sustainable agriculture have been discussed. This will help to make better decisions toward the productivity of sustainable agriculture. This review is an attempt to showcase the recent growth of bioinformatics databases and the role of big data analytics in achieving sustainable agriculture.
- Open Access
- 11 May 2026
- Published by Frontiers Media SA in Frontiers in Microbiology
- Vol. 17, 1862916
Editorial: Advanced biocatalysts for sustainable chemical synthesis
Waste materials, composed of excessive cross-linked disulfide bonds, pose serious environmental challenges and are difficult to process using the conventional proteases. Hence, a specific biocatalyst, keratinase, is the key player in biotransforming waste into a circular economy. However, the genuine biocatalyst was not efficient enough to achieve massive biotransformation. Hence, through the advent of genetic engineering tools, structural and functional properties were tailored to meet the targets of environmental remediation along with the industrial product. Researchers concluded that the research gap in utilising robust keratinases for waste material processing was addressed through the use of robust keratinase biocatalysts via diverse advancements including heterologous expression, artificial intelligence (AI)-assisted design, and muti-enzyme synergistic tools, to meet industrial requirement for bioprocessing various keratinaceous waste into value added products. Khider et al. (2026) have employed the genome editing tools, namely CRISPAR-CAS9, to improve the industrially significant thermophilic bacterium Bacillus methanolicus MGA3.Researchers constructed the pCasPP plasmid for efficient genome editing of target genes, namely katA, ald, and spo0A genes. Cas9 and sgRNA were induced to target double-strand breaks. Temperature regulation was selectively applied to the cleavage activity of Cas9 at 40 °C while 50 °C was utilized for DNA repair and further growth. The author reported the DNA repair mechanisms via two routes, namely homology-directed repair, and error-prone endjoining. Most interesting, three specific genes katA, ald, and spo0A, coding for catalase, alanine dehydrogenase, and sporulation regulator respectively, was validated using the genome editing tool with efficiencies exceeding 85% for deletions and 80-95% for gene substitution.Researchers have identified limitations, such as cas9 thermal sensitivity, secondary mutations, metabolic buffering/redundancy, and fitness cost that require further investigations.discovering a subfamily that is active on para-alkylated phenol derivatives to produce ketones.Alcohol oxidases are the important oxidoreductase class that catalyses the variety of phenol derivatives to alcohol, aldehydes, and ketones. However, beginning with para-alkyl substituted phenols, the ketones are often not accessible due to oxidases not functioning towards chiral benzylic alcohols. Researchers employed phylogenetic and amino acid clustering approaches to explore one clade having a significantly different active site constitution while retaining essential residues for catalysis. Researchers have chosen five candidates from this clade for investigation. One member, namely vanillyl oxidase (VAO) from Paecilomyces variotii (PvVAO), was found to possess unique properties that enable it to catalyse para-alkylated phenolic compounds to ketones. A new subfamily of fungal VAOs lacks the octamerization loop compared to existing known VAOs. These new VAOs possess unique enzymatic activities that catalyse the oxidative deamination of phenolic amines at pH> 9.0 and moreover, oxidise para-alkyl substituted phenols to valuable flavour ketones compounds. However, researchers identified areas such as lower specific activities, inactive proteins production, narrow pH stability and unique behaviour of lacking ether cleavage. Researchers pinpointed that the low activity with standard substrate indicates the enzyme may have evolved for bioconversion of other substrate that are yet to be identified as natural compounds.Yang et al. ( 2025) have demonstrated a bioprocess for the production of a nonprotein amino acid, namely 5-Aminolevulinic acid (5-ALA). Since 5-ALA is widely used in medicine, food, and agriculture industries, researchers employed a growth-coupled selection strategy improve 5-aminolevunic acid synthase (ALAS) sourced from Rhodobacter capsulatus using random and site-directed mutagenesis. The derived ALAS mutants were then introduced into the GRAS organism Corynebacteriun glutamicum. The best mutants yielded 1.18-fold higher product compared to the wild type. Bioprocess optimization led to the maximum production of the amino acid with a concentration of 8.72 g/L in 60 h. The fermentation optimization depended on key components such as dissolved oxygen, Fe 2+ , and glycine, which rendered maximum enzyme activity. Researchers successfully demonstrated product formation with the scope for further improvement in the present study, such as a better understanding of selection pressure bias in terms of lack of correlation between 5-ALA titres in liquid culture with biomass accumulation, better downstream processing for porphyrin production responsible for hampering 5-ALA accumulation, and finally, oxidative stress to the host organism of higher product formation.Song and Guo (2025) developed an effective methodology for the SUMO-fused recombinant protein expression system of human D-glucuronyl C5-epimerase (Glce) with a dimer structure in E. coli for better folding and solubility. The recombinant Glce is a key enzyme for the production of heparan sulphate proteoglycan. Researchers performed two N-terminal truncations, one at Glce167-617 and other at Glce102-617. However, the shorter construct Glce167-617 provided a higher protein expression level and purity of 98% compared to the longer constructs Glce102-617. Further, Researchers investigated the structural analysis of the protein Glce167-617 using X-ray crystallography and confirmed that the dimeric nature of protein in solution is due to the C-terminal alpha-barrel domain. Further, the enzyme retained evolutionary conserved substrate binding sites. However, researchers confirmed purity issues
- 11 May 2026
- Published by Frontiers Media SA in Frontiers in Microbiology
- Vol. 17, 1862916
Open AccessEditorial: Advanced biocatalysts for sustainable chemical synthesis
Waste materials, composed of excessive cross-linked disulfide bonds, pose serious environmental challenges and are difficult to process using the conventional proteases. Hence, a specific biocatalyst, keratinase, is the key player in biotransforming waste into a circular economy. However, the genuine biocatalyst was not efficient enough to achieve massive biotransformation. Hence, through the advent of genetic engineering tools, structural and functional properties were tailored to meet the targets of environmental remediation along with the industrial product. Researchers concluded that the research gap in utilising robust keratinases for waste material processing was addressed through the use of robust keratinase biocatalysts via diverse advancements including heterologous expression, artificial intelligence (AI)-assisted design, and muti-enzyme synergistic tools, to meet industrial requirement for bioprocessing various keratinaceous waste into value added products. Khider et al. (2026) have employed the genome editing tools, namely CRISPAR-CAS9, to improve the industrially significant thermophilic bacterium Bacillus methanolicus MGA3.Researchers constructed the pCasPP plasmid for efficient genome editing of target genes, namely katA, ald, and spo0A genes. Cas9 and sgRNA were induced to target double-strand breaks. Temperature regulation was selectively applied to the cleavage activity of Cas9 at 40 °C while 50 °C was utilized for DNA repair and further growth. The author reported the DNA repair mechanisms via two routes, namely homology-directed repair, and error-prone endjoining. Most interesting, three specific genes katA, ald, and spo0A, coding for catalase, alanine dehydrogenase, and sporulation regulator respectively, was validated using the genome editing tool with efficiencies exceeding 85% for deletions and 80-95% for gene substitution.Researchers have identified limitations, such as cas9 thermal sensitivity, secondary mutations, metabolic buffering/redundancy, and fitness cost that require further investigations.discovering a subfamily that is active on para-alkylated phenol derivatives to produce ketones.Alcohol oxidases are the important oxidoreductase class that catalyses the variety of phenol derivatives to alcohol, aldehydes, and ketones. However, beginning with para-alkyl substituted phenols, the ketones are often not accessible due to oxidases not functioning towards chiral benzylic alcohols. Researchers employed phylogenetic and amino acid clustering approaches to explore one clade having a significantly different active site constitution while retaining essential residues for catalysis. Researchers have chosen five candidates from this clade for investigation. One member, namely vanillyl oxidase (VAO) from Paecilomyces variotii (PvVAO), was found to possess unique properties that enable it to catalyse para-alkylated phenolic compounds to ketones. A new subfamily of fungal VAOs lacks the octamerization loop compared to existing known VAOs. These new VAOs possess unique enzymatic activities that catalyse the oxidative deamination of phenolic amines at pH> 9.0 and moreover, oxidise para-alkyl substituted phenols to valuable flavour ketones compounds. However, researchers identified areas such as lower specific activities, inactive proteins production, narrow pH stability and unique behaviour of lacking ether cleavage. Researchers pinpointed that the low activity with standard substrate indicates the enzyme may have evolved for bioconversion of other substrate that are yet to be identified as natural compounds.Yang et al. ( 2025) have demonstrated a bioprocess for the production of a nonprotein amino acid, namely 5-Aminolevulinic acid (5-ALA). Since 5-ALA is widely used in medicine, food, and agriculture industries, researchers employed a growth-coupled selection strategy improve 5-aminolevunic acid synthase (ALAS) sourced from Rhodobacter capsulatus using random and site-directed mutagenesis. The derived ALAS mutants were then introduced into the GRAS organism Corynebacteriun glutamicum. The best mutants yielded 1.18-fold higher product compared to the wild type. Bioprocess optimization led to the maximum production of the amino acid with a concentration of 8.72 g/L in 60 h. The fermentation optimization depended on key components such as dissolved oxygen, Fe 2+ , and glycine, which rendered maximum enzyme activity. Researchers successfully demonstrated product formation with the scope for further improvement in the present study, such as a better understanding of selection pressure bias in terms of lack of correlation between 5-ALA titres in liquid culture with biomass accumulation, better downstream processing for porphyrin production responsible for hampering 5-ALA accumulation, and finally, oxidative stress to the host organism of higher product formation.Song and Guo (2025) developed an effective methodology for the SUMO-fused recombinant protein expression system of human D-glucuronyl C5-epimerase (Glce) with a dimer structure in E. coli for better folding and solubility. The recombinant Glce is a key enzyme for the production of heparan sulphate proteoglycan. Researchers performed two N-terminal truncations, one at Glce167-617 and other at Glce102-617. However, the shorter construct Glce167-617 provided a higher protein expression level and purity of 98% compared to the longer constructs Glce102-617. Further, Researchers investigated the structural analysis of the protein Glce167-617 using X-ray crystallography and confirmed that the dimeric nature of protein in solution is due to the C-terminal alpha-barrel domain. Further, the enzyme retained evolutionary conserved substrate binding sites. However, researchers confirmed purity issues
- Open Access
- 29 August 2024
- Published by MDPI AG in Sustainability
- Vol. 16 (17) , 7496
Microbial Production of Biopesticides for Sustainable Agriculture
Food security is threatened by biotic stress on crops, e.g., from invasive pests, in the context of climate change. Pest control has traditionally been achieved using synthetic pesticides, yet pollution and the persistence and toxicity of some pesticides are inducing food contamination and, in turn, generating public concern. As a consequence, biopesticides are increasingly used, notably for organic crops. For instance, some microorganisms produce biopesticidal compounds such as secondary metabolites or growth-inhibitory enzymes. Most reviews on this topic mainly focus on describing microbial species and their active compounds. However, there are very few studies and reviews describing various process parameters. Here, we review both microbial biopesticides and factors controlling physicochemical conditions for the scaling up of biopesticide production. We present biopesticides from bacteria (e.g., Bacillus thuringiensis), algae, fungi, and viruses and review the biocontrol mechanisms and applications of commercial biopesticides. The benefits of genetic engineering for enhancing activity and drawbacks such as commercialization are also discussed.
- 29 August 2024
- Published by MDPI AG in Sustainability
- Vol. 16 (17) , 7496
Open AccessMicrobial Production of Biopesticides for Sustainable Agriculture
Food security is threatened by biotic stress on crops, e.g., from invasive pests, in the context of climate change. Pest control has traditionally been achieved using synthetic pesticides, yet pollution and the persistence and toxicity of some pesticides are inducing food contamination and, in turn, generating public concern. As a consequence, biopesticides are increasingly used, notably for organic crops. For instance, some microorganisms produce biopesticidal compounds such as secondary metabolites or growth-inhibitory enzymes. Most reviews on this topic mainly focus on describing microbial species and their active compounds. However, there are very few studies and reviews describing various process parameters. Here, we review both microbial biopesticides and factors controlling physicochemical conditions for the scaling up of biopesticide production. We present biopesticides from bacteria (e.g., Bacillus thuringiensis), algae, fungi, and viruses and review the biocontrol mechanisms and applications of commercial biopesticides. The benefits of genetic engineering for enhancing activity and drawbacks such as commercialization are also discussed.
- Open Access
- 28 December 2023
- Published by MDPI AG in Sustainability
- Vol. 16 (1) , 295
Bio-Nanoparticles Mediated Transesterification of Algal Biomass for Biodiesel Production
Immense use of fossil fuels leads to various environmental issues, including greenhouse gas emissions, reduced oil reserves, increased energy costs, global climate changes, etc. These challenges can be tackled by using alternative renewable fuels such as biodiesel. Many studies reported that biodiesel production from microalgae biomass is an environment-friendly and energy-efficient approach, with significantly improved fuel quality in terms of density, calorific value and viscosity. Biodiesel is produced using the transesterification process and the most sustainable method is utilizing enzymes for transesterification. Lipase is an enzyme with excellent catalytic activity, specificity, enantio-selectivity, compatibility and stability and hence it is applied in microalgae biodiesel production. But, difficulty in enzymatic recovery, high enzyme cost and minimal reaction rate are some of its drawbacks that have to be addressed. In this aspect, the nanotechnological approach of lipase immobilization in producing microalgae biodiesel is a promising way to increase production yield and it is due to the adsorption efficiency, economic benefit, recyclability, crystallinity, durability, stability, environmental friendliness and catalytic performance of the bio-nanoparticles used. Through increasing post-harvest biomass yield, absorption of CO2 and photosynthesis in the photobioreactor, the use of nanoparticle immobilized lipase during the generation of biodiesel from microalgae has the potential to also remove feedstock availability constraints. This review article discusses the production of microalgae biodiesel, and effect of nanoparticles and immobilized lipase nanoparticles on biodiesel production. The advantages of using lipase nanoparticles and the challenges in introducing the immobilized lipase on nanoparticles in large-scale microalgae biodiesel production are also discussed. Reducing the water and land use, energy and nutrient footprints of integrated algae-based operations must be the main goal of larger-scale experiments as well as ongoing research and development in order to expedite the adoption of microalgae-based biodiesel production. Also, the cost-effectiveness and large-scale availability of nanoparticles and the impact of lipase nanoparticles on engine performance should be analyzed for commercialization of microalgae biodiesel.
- 28 December 2023
- Published by MDPI AG in Sustainability
- Vol. 16 (1) , 295
Open AccessBio-Nanoparticles Mediated Transesterification of Algal Biomass for Biodiesel Production
Immense use of fossil fuels leads to various environmental issues, including greenhouse gas emissions, reduced oil reserves, increased energy costs, global climate changes, etc. These challenges can be tackled by using alternative renewable fuels such as biodiesel. Many studies reported that biodiesel production from microalgae biomass is an environment-friendly and energy-efficient approach, with significantly improved fuel quality in terms of density, calorific value and viscosity. Biodiesel is produced using the transesterification process and the most sustainable method is utilizing enzymes for transesterification. Lipase is an enzyme with excellent catalytic activity, specificity, enantio-selectivity, compatibility and stability and hence it is applied in microalgae biodiesel production. But, difficulty in enzymatic recovery, high enzyme cost and minimal reaction rate are some of its drawbacks that have to be addressed. In this aspect, the nanotechnological approach of lipase immobilization in producing microalgae biodiesel is a promising way to increase production yield and it is due to the adsorption efficiency, economic benefit, recyclability, crystallinity, durability, stability, environmental friendliness and catalytic performance of the bio-nanoparticles used. Through increasing post-harvest biomass yield, absorption of CO2 and photosynthesis in the photobioreactor, the use of nanoparticle immobilized lipase during the generation of biodiesel from microalgae has the potential to also remove feedstock availability constraints. This review article discusses the production of microalgae biodiesel, and effect of nanoparticles and immobilized lipase nanoparticles on biodiesel production. The advantages of using lipase nanoparticles and the challenges in introducing the immobilized lipase on nanoparticles in large-scale microalgae biodiesel production are also discussed. Reducing the water and land use, energy and nutrient footprints of integrated algae-based operations must be the main goal of larger-scale experiments as well as ongoing research and development in order to expedite the adoption of microalgae-based biodiesel production. Also, the cost-effectiveness and large-scale availability of nanoparticles and the impact of lipase nanoparticles on engine performance should be analyzed for commercialization of microalgae biodiesel.
- 31 October 2023
- Published by Springer Nature
- p. 23-34
Nanobiotechnological Routes in Lignocellulosic Waste Pre-treatment for Bio-renewables Production
- 31 October 2023
- Published by Springer Nature
- p. 23-34
Nanobiotechnological Routes in Lignocellulosic Waste Pre-treatment for Bio-renewables Production
- Open Access
- 19 October 2023
- Published by Frontiers Media SA in Frontiers in Microbiology
- Vol. 14, 1296573
Editorial: Microbial nanotechnology: a new frontier in microbiology
Editorial: Microbial nanotechnology: a new frontier in microbiology
- 19 October 2023
- Published by Frontiers Media SA in Frontiers in Microbiology
- Vol. 14, 1296573
Open AccessEditorial: Microbial nanotechnology: a new frontier in microbiology
Editorial: Microbial nanotechnology: a new frontier in microbiology
- 22 September 2022
- Published by Springer Nature in Physiology and Molecular Biology of Plants
- Vol. 28 (8) , 1
Correction to: TDZ-induced direct shoot organogenesis and somatic embryogenesis on cotyledonary node explants of lentil (Lens culinaris Medik.)
[This corrects the article DOI: 10.1007/s12298-008-0033-z.].
- 22 September 2022
- Published by Springer Nature in Physiology and Molecular Biology of Plants
- Vol. 28 (8) , 1
Correction to: TDZ-induced direct shoot organogenesis and somatic embryogenesis on cotyledonary node explants of lentil (Lens culinaris Medik.)
[This corrects the article DOI: 10.1007/s12298-008-0033-z.].