Production Of Industrial Enzymes Research Articles

Isolation of a novel Bacillus strain with industrial potential of producing alkaline chitosanase

A novel Bacillus strain, designated as HZ20-1, was discovered. This strain can produce naturally alkaline chitosanase without induction. Genomic analysis revealed that this chitosanase belongs to glycoside hydrolase family 8. When colloidal chitosan is used as a substrate, the maximum enzyme activity of 2.39 ± 0.03 U/mL is observed at a pH range of 8.5–9. This alkaline enzyme holds advantages over common acidic enzymes in various fields such as medicine, the environment, and daily chemical products, and thus has great market value. Moreover, as the chitosanase is a constitutive enzyme, there is no need for substrate induction. This can simplify fermentation equipment and reduce production cost. Additionally, in a preliminary study, we found that this strain can also degrade chitin and chitosan derivatives. After analysis, it was discovered that it has genes in glycoside hydrolase families 18 and 23. By controlling the enzymatic hydrolysis time, it is possible to produce products with different molecular weights, including N-acetylglucosamine, glucosamine, chito-oligosaccharides, and chitin oligosaccharides. Consequently, Bacillus sp. HZ20-1 is considered to have great potential for future industrial production of enzymes and oligosaccharides.

Characterization of a Polyphenol Oxidase and Lipase Produced by Microbes Derived from Palm Oil Sludge

Introduction: The waste-to-wealth concept was applied in this study. Our main objective was to identify and evaluate several microorganisms responsible for the production of important industrial enzymes using sludge from palm oil processing. We were able to isolate several bacteria that are tyrosinase producers: Bacillus cereus, Acinobacter seifertii, Klebsiella variicola and Pseudomonas stutzeri. Laccase producers Trametes polyzona, Bacillus subtilis, Bacillus pumilus and Staphylococcus condimenti, as well as lipase producers. Methods: In addition, we focused specifically on B. cereus because we knew that it produces tyrosinase. Lipase is another target enzyme, and S. condimenti was found to be a hyperproducer. Production conditions included a 24-hour incubation period at 40°C and a pH of 6.0, while typical substrates such as starch and coconut oil were used. Results: Preliminary protein purification studies identified a 43 kDa lipase that is active at pH 7.0 and 40°C. Salts such as NaCl, various detergents such as Triton X-100 and Tween-80 as well as many metal ions enhanced the activity and made the enzyme unique in its biological function. Conclusion: Even with EDTA (2.5 mM), which does not completely block its function, only 40% inhibition was observed. Only a few organic solvents such as butanol, acetone and DMF are involved in inhibiting its activity.

Multiple Regulatory Mechanisms Synergistically Control the Soluble Expression of CsCE for Enhanced Enzymatic Productivity of Lactulose in E. coli.

The limited expression of cellobiose 2-epimerase poses a significant constraint on the industrial enzymatic production of lactulose. Extensive modifications to the expression cassette offer a means to enhance the yield of recombinant proteins. In this study, an integrated strategy, combining individual and collaborative approaches, is proposed to fine-tune each stage of the CsCE overexpression program. This strategy involves the multidimensional integration of standardized genetic elements at various levels, including transcription, translation, folding, and three-dimensional structure. The volumetric activity of the final recombinant strain was markedly increased by 12-fold compared to the wild-type strain, reaching 2260.62 U/L. The protein expression in the newly developed high-yield recombinant strain exhibited a significant enhancement, with a higher proportion of soluble protein compared to that of inclusion bodies. Our findings offer insights into the multifaceted synergistic regulation of protein expression processes, holding promising implications for the production of heterologous recombinant proteins.

Review of the Proteomics and Metabolic Properties of Corynebacterium glutamicum.

Corynebacterium glutamicum (C. glutamicum) has become industrially important in producing glutamic acid and lysine since its discovery and has been the subject of proteomics and central carbon metabolism studies. The proteome changes depending on environmental conditions, nutrient availability, and stressors. Post-translational modification (PTMs), such as phosphorylation, methylation, and glycosylation, alter the function and activity of proteins, allowing them to respond quickly to environmental changes. Proteomics techniques, such as mass spectrometry and two-dimensional gel electrophoresis, have enabled the study of proteomes, identification of proteins, and quantification of the expression levels. Understanding proteomes and central carbon metabolism in microorganisms provides insight into their physiology, ecology, and biotechnological applications, such as biofuels, pharmaceuticals, and industrial enzyme production. Several attempts have been made to create efficient production strains to increase productivity in several research fields, such as genomics and proteomics. In addition to amino acids, C. glutamicum is used to produce vitamins, nucleotides, organic acids, and alcohols, expanding its industrial applications. Considerable information has been accumulated, but recent research has focused on proteomes and central carbon metabolism. The development of genetic engineering technologies, such as CRISPR-Cas9, has improved production efficiency by allowing precise manipulation of the metabolic pathways of C. glutamicum. In addition, methods for designing new metabolic pathways and developing customized strains using synthetic biology technology are gradually expanding. This review is expected to enhance the understanding of C. glutamicum and its industrial potential and help researchers identify research topics and design studies.

Gene function characterization in Aspergillus niger using a dual resistance marker transformation system mediated by Agrobacterium tumefaciens

Aspergillus niger is a well-known workhorse for the industrial production of enzymes and organic acids. This fungus can also cause postharvest diseases in fruits. Although Agrobacterium tumefaciens-mediated transformation (ATMT) based on antibiotic resistance markers has been effectively exploited for inspecting functions of target genes in wild-type fungi, it still needs to be further improved in A. niger. In the present study, we re-examined the ATMT in the wild-type A. niger strains using the hygromycin resistance marker and introduced the nourseothricin resistance gene as a new selection marker for this fungus. Unexpectedly, our results revealed that the ATMT method using the resistance markers in A. niger led to numerous small colonies as false-positive transformants on transformation plates. Using the top agar overlay technique to restrict false positive colonies, a transformation efficiency of 87 ± 18 true transformants could be achieved for 106 conidia. With two different selection markers, we could perform both the deletion and complementation of a target gene in a single wild-type A. niger strain. Our results also indicated that two key regulatory genes (laeA and veA) of the velvet complex are required for A. niger to infect apple fruits. Notably, we demonstrated for the first time that a laeA homologous gene from the citrus postharvest pathogen Penicillium digitatum was able to restore the acidification ability and pathogenicity of the A. niger ΔlaeA mutant. The dual resistance marker ATMT system from our work represents an improved genetic tool for gene function characterization in A. niger.

Efficient CRISPR-mediated C-to-T base editing in Komagataella phaffii.

The nonconventional methylotrophic yeast Komagataella phaffii is widely applied in the production of industrial enzymes, pharmaceutical proteins, and various high-value chemicals. The development of robust and versatile genome editing tools for K. phaffii is crucial for the design of increasingly advanced cell factories. Here, we first developed a base editing method for K. phaffii based on the CRISPR-nCas9 system. We engineered 24 different base editor constructs, using a variety of promoters and cytidine deaminases (CDAs). The optimal base editor (PAOX2*-KpA3A-nCas9-KpUGI-DAS1TT) comprised a truncated AOX2 promoter (PAOX2*), a K. phaffii codon-optimized human APOBEC3A CDA (KpA3A), human codon-optimized nCas9 (D10A), and a K. phaffii codon-optimized uracil glycosylase inhibitor (KpUGI). This optimal base editor efficiently performed C-to-T editing in K. phaffii, with single-, double-, and triple-locus editing efficiencies of up to 96.0%, 65.0%, and 5.0%, respectively, within a 7-nucleotide window from C-18 to C-12. To expand the targetable genomic region, we also replaced nCas9 in the optimal base editor with nSpG and nSpRy, and achieved 50.0%-60.0% C-to-T editing efficiency for NGN-protospacer adjacent motif (PAM) sites and 20.0%-93.2% C-to-T editing efficiency for NRN-PAM sites, respectively. Therefore, these constructed base editors have emerged as powerful tools for gene function research, metabolic engineering, genetic improvement, and functional genomics research in K. phaffii.

Production of Amylase Enzyme by Aspergillus and Fusarium Species using Sugar Cane Bagasse

Study’s Novelty/Excerpt This study presents insights into the cost-effective production of amylase enzymes using sugar cane bagasse as a substrate, showcasing a significant advancement over traditional synthetic starch substrates. By optimizing production parameters such as incubation time, substrate and inoculum concentrations, pH, and temperature, the research demonstrates the superior amylase yield of Aspergillus niger, Aspergillus flavus, and Fusarium spp. under specific conditions. This work not only highlights the potential of using waste materials for industrial enzyme production but also emphasizes the need for further exploration of the isolates' identities and the industrial applications of the extracted enzymes. Full Abstract Amylases are hydrolytic enzymes produced by some microorganisms and utilized in the hydrolysis of starch. This study aimed to determine the ability of certain fungal isolates isolated from wastes to synthesize the amylase enzyme utilizing synthetic soluble starch and sugar cane bagasse as substrates. Aspergillus niger, Aspergillus flavus, and Fusarium spp., previously identified to have amylolytic activity, were used for the research. The submerged fermentation process was used to produce amylase, with basal medium and sugar cane bagasse as substrates. The incubation time, substrate and inoculum concentrations, pH, and temperature were all optimized. The dinitrosalicylic acid reagent (DNS) technique was used to determine the activity of the amylase generated. Initial production of amylase using soluble starch (20 g (w/v)) as substrate at room temperature and pH 7.0 shows that all the isolates produce amylase better when their concentration (3%) is high but have different incubation periods of 96 hr for Aspergillus niger (8.65±0.21 U/mL/minutes) and Fusarium spp (7.15±0.07 U/mL/minutes), while Aspergillus flavus (7.30±0.14 U/mL/minutes) requires an extended incubation period of 144 hr to produce the product. Further production using sugar cane bagasse and optimization of production parameters of the isolates reveals that Aspergillus niger (4.35±0.07 U/mL/minutes) has an optimum incubation period of 120 hours, an inoculum concentration and substrate concentration of 2% each, and a pH of 6, Aspergillus flavus (6.40±0.28 U/mL/minutes) has an optimum incubation period of 144 hours, with inoculum and substrate concentration of 3% each at neutral pH, Fusarium spp (6.80±0.28 U/mL/minutes) has an optimum incubation period of 168hr., inoculum concentration of 3%, substrate concentration of 2% and a neutral pH-7 and all the isolates have their best yield at temperature of 30oC. In conclusion, using cheap and readily available sugar cane bagasse can be a more cost-effective option for expensive synthetic starch substrates used in amylase synthesis. The study suggests further investigation into the isolates' identities and the extracted enzyme's industrial application.

Secretion of the cytoplasmic and high molecular weight β-galactosidase of Paenibacillus wynnii with Bacillus subtilis

BackgroundThe gram-positive bacterium Bacillus subtilis is widely used for industrial enzyme production. Its ability to secrete a wide range of enzymes into the extracellular medium especially facilitates downstream processing since cell disruption is avoided. Although various heterologous enzymes have been successfully secreted with B. subtilis, the secretion of cytoplasmic enzymes with high molecular weight is challenging. Only a few studies report on the secretion of cytoplasmic enzymes with a molecular weight > 100 kDa.ResultsIn this study, the cytoplasmic and 120 kDa β-galactosidase of Paenibacillus wynnii (β-gal-Pw) was expressed and secreted with B. subtilis SCK6. Different strategies were focused on to identify the best secretion conditions. Tailormade codon-optimization of the β-gal-Pw gene led to an increase in extracellular β-gal-Pw production. Consequently, the optimized gene was used to test four signal peptides and two promoters in different combinations. Differences in extracellular β-gal-Pw activity between the recombinant B. subtilis strains were observed with the successful secretion being highly dependent on the specific combination of promoter and signal peptide used. Interestingly, signal peptides of both the general secretory- and the twin-arginine translocation pathway mediated secretion. The highest extracellular activity of 55.2 ± 6 µkat/Lculture was reached when secretion was mediated by the PhoD signal peptide and expression was controlled by the PAprE promoter. Production of extracellular β-gal-Pw was further enhanced 1.4-fold in a bioreactor cultivation to 77.5 ± 10 µkat/Lculture with secretion efficiencies of more than 80%.ConclusionFor the first time, the β-gal-Pw was efficiently secreted with B. subtilis SCK6, demonstrating the potential of this strain for secretory production of cytoplasmic, high molecular weight enzymes.

Genetic Engineering of Filamentous Fungi: Prospects for Obtaining Fourth-Generation Biological Products

Filamentous fungi exhibit unparalleled potential as cell factories for protein production, owing to their adeptness in protein secretion and remarkable proficiency in post-translational modifications. This review delineates the role of filamentous fungi in bio-input technology across different generations and explores their capacity to generate secondary metabolites. Our investigation highlights filamentous fungi as frontrunners in the production of bioactive compounds, emphasizing the imperative nature of elucidating their metabolic repertoire. Furthermore, we delve into common strategies for genetic transformation in filamentous fungi, elucidating the underlying principles, advantages, and drawbacks of each technique. Taking a forward-looking approach, we explore the prospects of genome engineering, particularly the CRISPR-Cas9 technique, as a means to propel protein secretion in filamentous fungi. Detailed examination of the protein secretion pathways in these fungi provides insights into their industrial applications. Notably, extensive research within the scientific community has focused on Aspergillus and Trichoderma species for the industrial production of proteins and enzymes. This review also presents practical examples of genetic engineering strategies aimed at augmenting enzyme secretion in filamentous fungi for various industrial applications. These findings underscore the potential of filamentous fungi as versatile platforms for protein production and highlight avenues for future research and technological advancement in this field.

Introduction of Cellulolytic Bacterium Bacillus velezensis Z2.6 and Its Cellulase Production Optimization.

Enzyme-production microorganisms typically occupy a dominant position in composting, where cellulolytic microorganisms actively engage in the breakdown of lignocellulose. Exploring strains with high yields of cellulose-degrading enzymes holds substantial significance for the industrial production of related enzymes and the advancement of clean bioenergy. This study was inclined to screen cellulolytic bacteria, conduct genome analysis, mine cellulase-related genes, and optimize cellulase production. The potential carboxymethylcellulose-hydrolyzing bacterial strain Z2.6 was isolated from the maturation phase of pig manure-based compost with algae residuals as the feedstock and identified as Bacillus velezensis. In the draft genome of strain Z2.6, 31 related cellulolytic genes were annotated by the CAZy database, and further validation by cloning documented the existence of an endo-1,4-β-D-glucanase (EC 3.2.1.4) belonging to the GH5 family and a β-glucosidase (EC 3.2.1.21) belonging to the GH1 family, which are predominant types of cellulases. Through the exploration of ten factors in fermentation medium with Plackett-Burman and Box-Behnken design methodologies, maximum cellulase activity was predicted to reach 2.98 U/mL theoretically. The optimal conditions achieving this response were determined as 1.09% CMC-Na, 2.30% salinity, and 1.23% tryptone. Validation under these specified conditions yielded a cellulose activity of 3.02 U/mL, demonstrating a 3.43-fold degree of optimization. In conclusion, this comprehensive study underscored the significant capabilities of strain Z2.6 in lignocellulolytic saccharification and its potentialities for future in-depth exploration in biomass conversion.

Aspergillus oryzae as a Cell Factory: Research and Applications in Industrial Production.

Aspergillus oryzae, a biosafe strain widely utilized in bioproduction and fermentation technology, exhibits a robust hydrolytic enzyme secretion system. Therefore, it is frequently employed as a cell factory for industrial enzyme production. Moreover, A. oryzae has the ability to synthesize various secondary metabolites, such as kojic acid and L-malic acid. Nevertheless, the complex secretion system and protein expression regulation mechanism of A. oryzae pose challenges for expressing numerous heterologous products. By leveraging synthetic biology and novel genetic engineering techniques, A. oryzae has emerged as an ideal candidate for constructing cell factories. In this review, we provide an overview of the latest advancements in the application of A. oryzae-based cell factories in industrial production. These studies suggest that metabolic engineering and optimization of protein expression regulation are key elements in realizing the widespread industrial application of A. oryzae cell factories. It is anticipated that this review will pave the way for more effective approaches and research avenues in the future implementation of A. oryzae cell factories in industrial production.

Isolation, characterization, and screening of yeast biodiversity for multi- hydrolytic enzymes

The current investigation was conducted with the objective of identifying yeasts that possess the ability to secrete a range of hydrolytic enzymes. Yeast isolates were collected from various samples, and the morphological characteristics of both the colony and yeast cells were examined. The capacity for enzyme production was assessed in multiple isolates by inoculating them in different media and quantifying their activities in terms of pectinase, amylase, urease, lipase, β-galactosidase, and protease. Out of a total of 42 yeast isolates, 30 displayed enzymatic activity. It is plausible that the yeast isolates obtained in this study hold potential for the production of industrial enzymes. Molecular identification techniques were employed to identify two isolates that exhibited multi-enzyme production and the highest enzyme activities. It was determined that these isolates belonged to two genera of yeasts, namely Pichia and Hanseniaspora. Specifically, isolate Y 16 was identified as Pichia kudriavizvii OL621856, while isolate Y 26 was identified as Hanseniaspora guillermondii OL621857 strains.

Application of Trametes pubescens for dye removal and biological pretreatment of sugarcane bagasse

AbstractSugarcane bagasse (SB) is an abundantly available agrowaste that is used extensively as a substrate for the production of different industrial enzymes. It is a renewable resource, rich in fermentable sugars. However, the presence of lignin makes it difficult for microbes to degrade it and so it is difficult to utilize it. Keeping in mind the role of white rot fungi in lignin degradation, Trametes pubescens MB89 was used in this study for the delignification of SB with the simultaneous production of laccase. The fungus was also used for the degradation of malachite green dye. A Box–Behnken design (BBD) was used to optimize variables affecting solid state fermentation of SB for laccase production. The leftover SB after fermentation was used for cellulase production by the thermophilic bacterium Neobacillus sedimentimangrovi UE25. The BBD depicted optimized conditions as 60% moisture, particle size 100 μ, 10 days’ incubation period, 450 μM CuSO4, and a temperature of 30 °C. The laccase titers of 1271 IU mL−1 were obtained under optimized conditions. Neobacillus sedimentimangrovi UE25 produced 4.574 IU mL−1 of endoglucanase and 1.812 IU mL−1 of β‐glucosidase by utilizing fungal pretreated SB. Scanning electron microscopy and Fourier transform infrared spectroscopy confirmed the impact of fungal cultivation on SB. Pores were observed after microbial pretreatment and there were changes in the morphological characteristics such as the pith and fiber of SB. To test the ability of laccase to break down aromatic dyes, we grew the fungus T. pubescens MB89 in a nutrient‐rich medium supplemented with malachite green dye. The fungus was able to remove 73.68% of the malachite green dye from the medium in 24 h. This shows that T. pubescens MB89 has a range of potential applications for environmental and industrial purposes.

Implications of carbon catabolite repression for Aspergillus-based cell factories: A review.

Carbon catabolite repression (CCR) is a global regulatory mechanism that allows organisms to preferentially utilize a preferred carbon source (usually glucose) by suppressing the expression of genes associated with the utilization of nonpreferred carbon sources. Aspergillus is a large genus of filamentous fungi, some species of which have been used as microbial cell factories for the production of organic acids, industrial enzymes, pharmaceuticals, and other fermented products due to their safety, substrate convenience, and well-established post-translational modifications. Many recent studies have verified that CCR-related genetic alterations can boost the yield of various carbohydrate-active enzymes (CAZymes), even under CCR conditions. Based on these findings, we emphasize that appropriate regulation of the CCR pathway, especially the expression of the key transcription factor CreA gene, has great potential for further expanding the application of Aspergillus cell factories to develop strains for industrial CAZymes production. Further, the genetically modified CCR strains (chassis hosts) can also be used for the production of other useful natural products and recombinant proteins, among others. We here review the regulatory mechanisms of CCR in Aspergillus and its direct application in enzyme production, as well as its potential application in organic acid and pharmaceutical production to illustrate the effects of CCR on Aspergillus cell factories.

Novel Fungal Co-Culture Technique for Enhanced Bioconversion of Agro-Industrial Waste to Amylase

Global strategies for management of solid waste occasionally lead to the environmental pollution. Now a days environmental friendly methods to valorize this waste are more demand to reduce the global warming. Solid-state fermentation (SSF) which is a potential waste recycling method to convert these solid wastes into value-added products by microbial population. In the present study, SSF was carried out using four substrates namely castor husk, rice husk, groundnut fodder, sugarcane bagasse and saw dust for the selection of renewable and chief substrate for the industrial production of amylase enzyme. We used two indigenous strains i.e., Aspergillus protuberus and Aspergillus unguis. Maximum production of α-amylase 1.614 U/g of substrate and 0.958 U/g of substrate on 2nd day of incubation in rice husk respectively. Groundnut waste (0.847 U/g of substrate) and castor husk (0.692 U/g of substrate) were also showed highest production of glucoamylase on 1st day and 2nd day of incubation in SSF. Further, prominent increase in the production of α-amylase (12 U/ml) and glucoamylase (3 U/ml) and extra cellular secretion of protein (20 mg/ml) was noticed in co-culture system on 2nd day of incubation in submerged fermentation (SmF).

CRISPR/Cas9 improves targeted knock-in efficiency in Aspergillusoryzae

Aspergillus oryzae is an important fungus in food and industrial enzyme production. In A. oryzae, targeted knock-in transformation is primarily limited to homologous recombination (HR)-based systems, in which non-homologous end-joining (NHEJ)-disruptant hosts are required. However, preparation of hosts and transformation templates for such systems is laborious, in addition to other disadvantages. In the present study, we examined alternative targeted knock-in mediated by CRISPR/Cas9, in which a microhomology-mediated end-joining (MMEJ) and single-strand annealing (SSA) repair system was employed. This approach enabled the efficient development of targeted knock-in transformants without host preparation using only a short homology template. We conclude that this new method could be applied to facilitate the transformation of A. oryzae, and will make it easier to acquire targeted knock-in transformants, especially from industrially important non-model strains.

Biodegradation of Cassava Flour Production Wastes in the Brazilian Industry for Industrial Glycohydrolase Enzymes Production by Aspergillus niger

Biodegradation of Cassava Flour Production Wastes in the Brazilian Industry for Industrial Glycohydrolase Enzymes Production by Aspergillus niger

Valorization of agro-industrial wastes using fungi for industrial enzymes production

Huge quantities of the agricultural wastes are produced from practices related to industrial processing, which are mainly burned and thrown in landfills, becoming a threat to the human health and causing environmental pollution. Agro-industrial residues, such as sugarcane bagasse, orange peel, wheat bran, corn straw, barley, rice straw, corn cob, husk, soy bran, and coffee husk were considered as valuable raw materials that can be converted into products of biotechnological interest using microorganisms. Agro-industrial wastes rich in nutrients, such as proteins, minerals, and sugars that, used as possible low cost substrates, for the fungal cultivation, thus considered as an alternative eco-friendly tool for many biological products of economic value, such as enzymes. Fungi organisms are capable of synthesizing a wide range of relevant oxidative and hydrolytic extracellular enzymes, such as peroxidases, laccases, xylanases, and cellulases. The enzymes secreted fungi, are proteins that function as bio-catalysts, responsible for carrying out various biochemical reactions, which applied in food, detergent, cellulose, paper, cosmetics and textile industries, etc. Thus, the replacement of raw materials with lignocellulosic-sources can result in reducing environmental problems and resolving the pollution associated with their disposal, in addition a higher investment will be gained. Therefore, a review was carried out on the important value of agro-industrial wastes, and the cultivation of fungal isolates for economic production of the industrially important enzymes, based on submerged and solid-state fermentation processes, as well as the important application of these enzymes.

Industrial enzyme production in Bangladesh: current landscape, scope, and challenges

Enzymes are important biological catalysts that perform specialized functions within living organisms. Industrial enzymes are crucial in various sectors, including pharmaceuticals, the textile industry, the manufacturing of chemicals, biodiesel, the food and beverages industry, and consumer goods. Enzymes can be obtained from multiple sources, including microbes, animals, and plants. Microorganisms, especially bacteria and fungi, provide more than 50% of industrial enzymes because of their advantageous growth features, low nutritional needs, and biochemical diversity. Bangladesh's economy relies heavily on agriculture and generates biomass energy from waste such as rice husk, straw, jute sticks, and sugarcane bagasse. To reduce the environmental impact, it is vital to modify these waste materials into beneficial industrial and commercial products, like enzymes. This review article investigates the current landscape, scope, and challenges of industrial enzyme production in Bangladesh. Bangladesh has become an appealing destination for biotech firms due to variables such as yearly bio-product imports, local market consumer demand, and the availability of resources and competent people. In 2021, Bangladesh ranked as the 34th largest importer of enzymes worldwide, with an import value of $47.4 million. Bangladesh mainly imports enzymes from Turkey, Malaysia, China, Singapore, and Sri Lanka. This study identifies a critical research gap, which is the lack of a dedicated industrial enzyme production industry in Bangladesh. This gap is impeding large-scale implementation, despite ongoing research efforts. Furthermore, we suggest the establishment of a specialized industrial enzyme production sector in Bangladesh, which would benefit the environment and promote economic growth through the utilization of agro-industrial waste resources. Finally, this thorough assessment of current industrial enzyme research in Bangladesh seeks to provide researchers and stakeholders with essential information for future development. Collaboration between the government, businesses, and academics is critical to fostering growth and capitalizing on the potential of the worldwide enzyme industry. Asian J. Med. Biol. Res. 2023, 9 (4), 145-159

Trichoderma orarium (Hypocreales): a new species from Taiwan

Trichoderma spp. are widely distributed worldwide. Members of Trichoderma have been shown to play a significant role in the biocontrol of plant disease, as well as the industrial production of enzymes and antibiotics, and as a mycoparasite of edible fungi. In this study, a new species, Trichoderma orarium, is introduced and illustrated. This new species was isolated from coastal soil in Northeastern Taiwan and identified based on morphological characteristics and multi-gene sequence analyses of three loci (ITS, tef1, and rpb2). The phylogenetic analyses revealed that T. orarium belongs to the Harzianum clade. Distinctions between the new species and its close relatives are discussed in detail.