Enzyme Production Research Articles

Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis

BackgroundBacillus subtilis is widely used for industrial enzyme production due to its capacity to efficiently secrete proteins. However, secretion efficiency of enzymes varies widely, and optimizing secretion is crucial to make production commercially viable. Previously, we have shown that overexpression of the xylanase XynA lowers expression of Clp protein chaperones, and that inactivation of CtsR, which regulates and represses clp transcription, increases the production of XynA. In the current study, we examined whether the same is the case for overexpression of the α-amylase AmyM from Geobacillus stearothermophilus by B. subtilis, and why XynA shows a different timing of secretion compared to AmyM.ResultsTranscriptome analyses revealed that B. subtilis cells overexpressing AmyM exhibited a distinct profile compared to XynA overexpressing cells, however there were also similarities and in both cases expression of CtsR controlled genes was downregulated. In contrast to XynA, inactivation of CtsR did not improve AmyM production. Upregulation of other protein chaperones, including GroEL/ES and DnaJ/K, by inactivating their transcriptional repressor HrcA, had almost no effect on XynA yields and in fact considerably lowered that of AmyM. Despite using the same promoter, the production of XynA peaks well before AmyM reaches its optimal secretion rate. Transcriptome and ribosome profiling indicated that this is neither related to transcription nor to translation regulation. We show that the reduced secretion in the stationary phase is partially due to the activity of secreted proteases, but also due to the activity of the intracellular protease LonA. The absence of this protein resulted in a 140% and 20% increased production for XynA and AmyM, respectively.ConclusionThe combination of transcriptome and ribosome profiling offered important information to determine at which cellular level production bottlenecks occurred. This helped us to identify LonA protease as an important factor influencing enzyme production yields in B. subtilis.

Genome Analysis of a Polysaccharide-Degrading Bacterium Microbulbifer sp. HZ11 and Degradation of Alginate

Marine bacteria are crucial sources of alginate lyases, which play an essential role in alginate oligosaccharide (AOS) production. This study reports the biochemical characteristics of a new species of the Microbulbifer genus, Microbulbifer sp. HZ11. The strain HZ11 is Gram-negative, aerobic, flagellate-free, and rod-shaped. The genome of strain HZ11 is a 4,248,867 bp circular chromosome with an average GC content of 56.68%. HZ11 can degrade alginate and other polysaccharides. The carbohydrate-active enzyme (CAZyme) genes account for 4.57% of the total protein-coding genes of HZ11. Its alginate metabolism process is consistent with the characteristics of the polysaccharide utilization locus (PUL) system. The alginate lyase produced by strain HZ11 showed the highest activity at 50 °C, pH 8.5, and 0.1 M NaCl. The substrate preference was as follows: sodium alginate > poly mannuronic acid > poly guluronic acid. The thin layer chromatography (TLC) results revealed that the main enzymatic degradation products were monosaccharides or AOSs with a degree of polymerization (DP) of 2–3. These results help clarify the metabolism and utilization mechanism of alginate by marine bacteria and provide a theoretical reference for its application in the degradation of alginate and other polysaccharides.

Whole genome analysis, detoxification of ochratoxin a and physiological characterization of a novel Bacillus velezensis MM35 isolated from soil

Ochratoxin A (OTA) is a significant global contaminant that poses severe challenges to food safety and public health. This study aims to isolate the OTA-degrated probiotics and evaluate genetic and biological characteristic. Here, The degradation rate of a new strain named Bacillus velezensis MM35 isolated from soil was the highest (87.10% within 48 h), and its culture supernatant was the main component of OTA degradation (63.95%) by high performance liquid chromatography. Further investigation revealed that the extracellular enzyme that degrades OTA in the culture supernatant of MM35 may be a small molecule enzyme with certain heat resistance. Genome-wide analysis showed that MM35 contains a cluster of carboxypeptidases encoding OTA-degrading potential, and had good metabolic and catalytic synthesis ability, and strong application potential in the synthesis and degradation of carbohydrates and proteins. A variety of secondary metabolites with antibacterial properties, such as non-ribosomal peptide synthetase and terpenoids, were identified in its metabolites. Consistent with the predicted results, MM35 showed various enzyme production characteristics such as cellulase and xylanase. Furthermore, MM35 could inhibit the growth of a variety of pathogenic bacteria, and showed high co-aggregation ability to Escherichia coli and Salmonella typhimurium. In addition, MM35 has certain tolerance to harsh environments such as strong acid, bile salt, and high temperature. Additionally, the adhesion rate of MM35 was 5.4%, and the invasion rate was 2.1% in IPEC-J2 cells. In summary, the data suggest MM35 isolated strain has high OTA degradation efficiency, antibacterial activity and intestinal colonization, which provided a new way for the treatment of OTA contamination in food and feed industries.

Biosynthesis of Bacteriochlorophylls and Bacteriochlorophyllides in Escherichia coli.

Photosynthesis, the most important biological process on Earth, converts light energy into chemical energy with essential pigments like chlorophylls and bacteriochlorophylls. The ability to reconstruct photosynthesis in heterotrophic organisms could significantly impact solar energy utilization and biomass production. In this study, we focused on constructing light-dependent biosynthesis pathways for bacteriochlorophyll (BChl) a and bacteriochlorophyllide (BChlide) d and c in the model strain Escherichia coli. The production of the starting compound, Mg protoporphyrin monomethylester, was optimized by screening the ribosome binding sites for the expression of each of the five genes. By fusing a maltose-binding protein and apolipoprotein A-I domain with the membrane protein BchF, the yield of 3-hydroxyethyl-Chlide a was increased by five-fold. Anaerobic cultivation of the engineered E. coli strains facilitated the reduction of the C7=C8 double bond by chlorophyllide a oxidoreductase, a critical step in BChl a synthesis. We further enhanced BChl a production by adjusting the isopropyl-β-d-thiogalactopyranoside concentration to optimize enzyme production and introducing an exogenous superoxide dismutase to combat oxidative stress. Additionally, fusing BciC with a RIAD tag resulted in an eight-fold increase in the production of 3-vinyl BChlide d. This study lays the foundation for the reconstitution of BChl-based photosynthetic apparatus in heterotrophic model organisms, offering promising avenues for future research and applications in biotechnology.

Genetic Engineering Pharmaceutical Technology: A Brief Review

Genetic engineering has emerged as a transformative technology in the pharmaceutical industry, offering unprecedented control over the manipulation of genetic material. This technology enables the precise editing, combining, and expression of target genes in various organisms, leading to the production of specific proteins, enzymes, and biologics essential for therapeutic applications. This review provides an overview of the basic principles and strategies of gene therapy, the development of genetic engineering pharmaceuticals, and their applications in producing physiologically active substances, antibodies, and vaccines. The review also highlights the significant advancements in the field, and explores the future potential of genetic engineering in advancing medical science and improving human health.

Screening, Identification, and Optimization of Enzyme Production for Bacteria with High Efficiency of Bovine Blood Protein Degradation from Slaughterhouses

Blood waste originating from slaughterhouse activities in China is considered to be massive, and improper handling may cause epidemic diseases and environmental pollution. This research aimed to obtain a potential bacterial strain for blood protein degradation by isolating indigenous bacteria from slaughterhouses. Isolation was carried out by using dilution plate coating, while blood agar and casein plates were used to screen potential strains. Morphological, physiological, and biochemical characterizations, as well as 16S rRNA sequencing, were performed to identify the selected strain. The optimization of enzyme production was performed by using the Plackett–Burman test and response surface methodology. A strain coded NwMCC01910137 was isolated and screened to effectively degrade bovine blood protein and was identified as Bacillus subtilis. The optimum culture conditions for enzyme production included a fermentation temperature of 37.4 °C, an initial pH of 7.7, a soybean meal powder addition amount of 3.00% (w/v), a glucose level of 3.8% (w/v), a NaCl level of 0.3 g/L, a phosphate concentration of 2.5 g/L, an inoculum size of 2.5 g/L (4%), and a fermentation time of 48 h. Under the optimum condition, the strain showed enzyme activity of 166.83 U/mL. Hence, the isolated B. subtilis showed good activity in bovine blood protein degradation and has good application potential for slaughterhouse waste processing.

Enhanced production of thermostable catalase for efficient gluconic acid biocatalysis

IntroductionThe demand for gluconic acid (GA) has risen recently, driven by its extensive applications in the food, healthcare, and construction industries. The biocatalysis of gluconic acid, facilitated by glucose oxidase and catalase, hinges on enzyme stability, significantly influencing catalytic efficiency. Nonetheless, catalase requires enhancements in thermal stability and activity to meet the requirements of practical applications.MethodsWe evaluated ten catalases expressed in Aspergillus niger, ultimately selecting the catalase from the thermophilic fungus Thermoascus aurantiacus, labeled as TaCat, for its superior thermal stability and operational performance. We further characterized the enzymatic properties of the recombinant catalase, focusing on its thermostability. Simultaneously, we used AlphaFold2 for structural predictions and conducted in-depth analyses via accelerated molecular dynamics simulations.Results and discussionWe successfully obtained a strain with the highest catalase activity by optimizing signal peptides and overexpressing the crucial heme synthesis enzyme. Enzyme production reached an impressive 321,779.5 U/mL in a 50-L fermenter. Our application studies confirmed the considerable advantages of TaCat in terms of GA production. In conclusion, TaCat, distinguished by its remarkable thermal stability and high activity, holds substantial potential for GA production.

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Paddy residues burning is a common practice in the sub-continent to manage paddy waste,which results in deterioration of air quality in the surrounding areas and causes smog issue. In situ decomposition could be a viable option to manage this problem. About thirteen (13) cellulose degrading bacterial strains were selected and further screened based on various enzymatic activities. Finally, two strains (GW7 and HA 121) with highest enzymatic potential were selected for optimization of factors to enhance cellulase production. The selected bacterial strain GW7 was found positive for urease, protease, catalase, phosphates and cellulase activity. While HA121 strain was positive for urease, protease, phosphatase and cellulase enzymes. The strains GW7 and HA121 exhibited maximum cellulose activity of 23 U mL-1 and 19 U mL-1, respectively, at optimized conditions. The optimal conditions for GW7 were temperature 35°C, pH 8, 1.5% glucose and 0.5% urea concentration. However, for HA121 the highest cellulase activity was attained when 1% glucose and 0.5% urea as co-inducers were used at a temperature of 35 °C and pH 8 where cellulase enzyme production was found to be 19 U mL-1. The optimization of cellulolytic bacterial cultures for enhanced cellulase production has established its potential utilization for field application.

Mining, Identification, and Fermentation Optimization of Chitin Deacetylase from a Novel Strain Enterobacter sp. ZCDA27.

Chitin, a natural organic compound with content slightly lower than cellulose, is also known for chitosan, a substance derived from chitin through deacetylation. In this experiment, preliminary screening was conducted using the plate discoloration circle method, leading to the selection of a high-yield CDA-producing strain from 28 candidates through rescreening. Morphological characteristics and 16S rDNA sequence analysis revealed 99.93% homology with Enterobacter sichuanensis strain N24, thus naming this strain Enterobacter strain ZCDA27. Initial fermentation of the strain yielded CDA activity of 9.29 U/mL. Single-factor optimization was then performed, followed by a PB test to screen for significant factors affecting enzyme production. The response surface method was used to further optimize the fermentation conditions. The optimal fermentation conditions for the carbon source, nitrogen source, metal ion, fermentation temperature, time, liquid volume, and initial pH were explored. Significant factors affecting enzyme production, including MgSO4, initial medium pH, and fructose levels, were identified using the PB test. Finally, the fermentation conditions of ZCDA27 were optimized using the Box-Behnken design combined with RSM, which comprised fructose at 1.020%, magnesium sulfate at 0.016%, and peptone at 1%. The fermentation conditions included a temperature of 37, initial pH of 7.1, rotation speed of 140 × g, fermentation time of 28h, inoculation amount of 2%, and liquid volume of 40%. Under these conditions, the enzyme activity of ZCDA27 reached 14.52 U/mL, a 1.6-fold increase from the pre-optimization levels. In summary, this study provides an experimental foundation for further development and application of Enterobacter spp. ZCDA27 CDA.

Exploring ultraviolet and nitrous acid-induced mutagenesis of Rhizopus oligosporus for extracellular inulinase production under solid-state culture.

This study details the synthesis and optimization of extracellular inulinase through solid-state fermentation using improved strain of Rhizopus oligosporus. The wild-type was procured from IIB culture bank and subsequently enhanced through UV-radiation and Nitrous acid treatments. The resulting mutant strain was subjected to further optimization for heightened enzyme production via solid-state fermentation. The substrate, pressmud (20g), and moisture content (20 mL molasses) were carefully selected. Key parameters such as inoculum size, incubation time, and inulin concentration were optimized to maximize enzyme yield. Mutation procedures involved optimizing spore suspension, UV-radiation exposure duration, and the distance of culture plate from UV rays. Nitrous acid treatment, followed by resistance development using L-cysteine HCl, further refined the mutant strains. Evaluation through UV-Vis spectrophotometry and comprehensive characterization using SEM, FTIR, and XRD were conducted to compare the results between the wild-type and mutant strains. The mutant strain exhibited significantly higher inulinase activity (111 ± 0.49 U/ml) as compared to its wild-type counterpart (59 ± 0.65 U/ml), indicating successful enhancement through the applied mutation techniques. The molecular weight of the inulinase enzyme produced from mutant strain and wild-type was 83 and 86kDa respectively. These findings suggest potential industrial applications of the improved strain in various biotechnological processes.

Genomic Characterization of Bacillus sp. THPS1: A Hot Spring-Derived Species with Functional Features and Biotechnological Potential

Bacillus sp. THPS1 is a novel strain isolated from a high-temperature hot spring in Thailand, exhibiting distinctive genomic features that enable adaptation to an extreme environment. This study aimed to characterize the genomic and functional attributes of Bacillus sp. THPS1 to understand its adaptation strategies and evaluate its potential for biotechnological applications. The draft genome is 5.38 Mbp with a GC content of 35.67%, encoding 5606 genes, including those linked to stress response and sporulation, which are essential for survival in high-temperature conditions. Phylogenetic analysis and average nucleotide identity (ANI) values confirmed its classification as a distinct species within the Bacillus genus. Pangenome analysis involving 19 others closely related thermophilic Bacillus species identified 1888 singleton genes associated with heat resistance, sporulation, and specialized metabolism, suggesting adaptation to nutrient-deficient, high-temperature environments. Genomic analysis revealed 12 biosynthetic gene clusters (BGCs), including those for polyketides and non-ribosomal peptides, highlighting its potential for synthesizing secondary metabolites that may facilitate its adaptation. Additionally, the presence of three Siphoviridae phage regions and 96 mobile genetic elements (MGEs) suggests significant genomic plasticity, whereas the existence of five CRISPR arrays implies an advanced defense mechanism against phage infections, contributing to genomic stability. The distinctive genomic features and functional capacities of Bacillus sp. THPS1 make it a promising candidate for biotechnological applications, particularly in the production of heat-stable enzymes and the development of resilient bioformulations.

Diversificación de las fuentes de nitrógeno para mejorar la actividad de esterasa durante la degradación del disruptor endocrino di(2-etilhexil) ftalato por Fusarium culmorum

Di(2-ethylhexyl) phthalate (DEHP) is the most used plasticizer, which is an environmental contaminant and is reported to be an endocrine disruptor in mammals. In this research, the effect of different nitrogen sources (urea, sodium nitrate and magnesium nitrate) on the growth and esterase produced by Fusarium culmorum during the degradation of DEHP (1500 mg/L) under submerged fermentation was evaluated. Growth kinetic and enzyme yields parameters were also estimated. These results showed that DEHP induced esterase production by F. culmorum and esterase production showed a nitrogen source-dependent pattern. Number and molecular weight of esterases were similar in the different nitrogen sources analyzed, however, magnesium nitrate was the best nitrogen source for esterase production (21651 U/L), followed by urea (13460 U/L), and sodium nitrate (3762 U/L). Two esterase isoforms appeared during the first 36 h with an average molecular weight of 26 and 32.6 kDa, which might be responsible for the primary DEHP degradation and the rest of the esterases which appeared after 48 h might be involved in the final steps of the biodegradation. Development of new strategies to increase enzyme production is crucial to establish efficient methods for DEHP biodegradation to mitigate the effects of DEHP pollution and the risk of health impacts.

Assessment of Phytochemical Compounds, Enzyme Production, and Antifungal, Antioxidant, and Anti-mutagenic Activities in Endophytic Fungi Derived from Mangrove Trees

Mangrove forest is a unique wetland ecosystem that is highly productive and provides an environment for a variety of microorganisms. Endophytic fungi derived from mangrove plants provide the plants with protection from adverse environmental conditions, while also allowing the fungi to produce valuable bioactive compounds. The present study sampled 11 mangrove trees and isolated, screened, and identified the potent endophytic fungi and their bioactive substances showing anti-pathogenic, anti-mutagenic and antioxidant activities, while the endophytes were investigated for their enzymatic potential. In total, 47 endophytic fungi were isolated from the leaves (36) and stems (11) of the host plants and all isolates were tested for antagonistic activities against selected plant pathogens. Based on the results, isolates BgS-04 and BcL-05 had the highest anti-pathogenic activities against Curvularia sp., Fusarium sp., and Colletotrichum sp. Therefore, the ethyl acetate crude extracts from these two fungi were further investigated for their antioxidant and anti-mutagenic activities and their phenolic compound contents, based on phytochemical analysis. Based on the results, the crude extracts of BgS-04 and BcL-05 contained 5.24 and 4.8 mg gallic acid equivalent/g of total phenolic compounds, respectively, and had antioxidant activity (half maximal inhibitory concentration) levels of 7.4 and 4.26 mg/mL, respectively. The preliminary qualitative phytochemical analysis of the fungal crude extracts identified tannins and coumarins. The anti-mutagenic activity levels of BgS-04 and BcL-05 against the mutagenic compounds, Trp-P-1 and DMBA, were determined using the Ames test, which revealed that the crude extracts of BgS-04 and BcL-05 had moderate-to-high antimutagenic potential against TA98 and TA100.All 47 endophytic isolates were assessed for their potential role in producing extracellular enzyme; they were capable of producing protease (53%), pectinase (28%), amylase (26%) and cellulase (19%) but none of them produced lipase. Among the isolates, RmL-01 derived from the leaves of Rhizophora mucronata had the significantly highest amylase production. Maximum amylase production (141.2 U/mL) was observed at 30 °C, pH 7.0 and 120 hours of incubation time. Molecular identification of the isolates BgS-04, BcL-05 and RmL-01 using nuclear ribosomal DNA internal transcribed spacer sequences revealed that they were Pestalotiopsis parva, Collectotrichum perseae, and Aspergillus oryzae, respectively, with high bootstrap support. It was concluded that the distinct groups of mangrove endophytes were potential sources of novel and valuable bio-based compounds with impressive anti-plant pathogen, anti-mutagenic, and antioxidant activities and capable of producing multi-industrial enzyme cocktails that might be important and useful for biotechnological applications.

A Component of the Septation Initiation Network Complex, SepL, Participates in the Cellobiose-Responsive Expression of Cellulolytic Enzyme Genes in Aspergillus aculeatus.

The production of cellulolytic enzymes in Aspergillus aculeatus is regulated at transcriptional levels in response to inducers and various physiological signals. In this study, we identified that a component of the septation initiation network complex, SepL, a putative protein kinase, was involved in the expression of carbohydrate-active enzyme (CAZyme) encoding genes. The deletion of sepL (ΔsepL) in A. aculeatus resulted in a deficiency in both septation and conidiation and sensitivity to Congo red. These phenotypes of ΔsepL are conserved in Aspergillus. In addition to the conserved function of SepL in Aspergillus, we found that SepL in A. aculeatus was necessary for the inducible expression of the CAZyme genes in response to cellobiose, whereas the inducible expression of these genes in response to 1,4-β-mannobiose was significantly reduced but not abolished. Combining the results of the present functional analysis of SepL with previous evidence that the expression of the CAZyme genes, which is responsive to both cellobiose and 1,4-β-mannobiose, is regulated by a transcription factor ManR in A. aculeatus, indicates that SepL in A. aculeatus is involved in the selective expression of the cellobiose-responsive CAZyme genes under the control of ManR.

Production, Screening and Purification of a Fibrinolytic Enzyme (Actinokinase) from Streptomyces species

Production, Screening and Purification of a Fibrinolytic Enzyme (Actinokinase) from Streptomyces species

Preparation of wheat germ albumin polypeptide microcapsules embedded with starch sodium octenylsuccinate/sodium alginate-based materials and sustained-release properties in vitro

The enzymatic hydrolysis products of wheat germ albumin have been extensively studied due to their strong antioxidant properties. The small intestine is an important part for absorbing active substances, but polypeptides are not acid-resistant and are easily hydrolyzed and lose their activity in the stomach, which does not achieve the effect of small intestine absorption. In this study, the optimal process conditions for microencapsulation of wheat germ albumin polypeptides were determined based on response surface optimization experiments as follows: wall to material ratio (starch sodium octenylsuccinate (SSOS) : sodium alginate (SA) =3:1), homogenization time 10 min, and wall to core ratio 20:1. The embedding rate of microcapsules prepared under these conditions was 65.33%. The average particle size of microcapsules was 100.21 μm. SEM results showed that the freeze-drying microcapsules had a sheet-like structure. The increased intensity of the amide A band in the microcapsules in Fourier transform infrared (FT-IR) spectroscopy indicated the formation of hydrogen bonds between the wall materials, while thermogravimetric analysis confirmed the protective effect of microcapsules on the formation of wheat germ albumin polypeptides. The release rates of microcapsules in gastric and intestinal juice were 26.54% and 84.41%, respectively, indicating that microcapsules had a sustained release effect.

Construction of template-free amplification system coupled with capillary electrophoresis for the simultaneous detection of three tumor-associated DNA repair enzymes

DNA repair enzymes are important in the repair of DNA lesions for maintaining the genome stability, and their abnormal expression induced various human cancers. Simultaneous detection of these DNA enzymes could provide convincing evidence based on the comparison of the activity of multiple enzymes than on that of single enzyme. Although fluorescence approach has been applied for the simultaneous detection both of DNA repair enzymes, the spectral overlap and multiwavelength excitation severely restrict the number of available fluorophores. Thus, it is difficult to simultaneously detect three enzymes in a single analysis by fluorescence detection. Herein, we developed a method for the simultaneous determination of three DNA repair enzymes including human flap DNA endonuclease 1 (FEN1), human alkyladenine DNA glycosylase (hAAG) and uracil DNA glycosylase (UDG) based on the combination of template-free amplification system with capillary electrophoresis-laser induced fluorescence (CE-LIF) detection. The amplification system was adopted to transfer and amplify the enzymatic products into different length DNA fragments which could be separated effectively by CE-LIF without the complicated modification of the capillary inner wall or labeling different tails on signal probes for separation. The method demonstrated a detection limit of 0.07 U/mL (0.08-160 U/mL) for FEN1, 2.40 U/mL (2.5-250 U/mL) for hAAG and 2.1 × 10−4 U/mL (0.0004-2.5 U/mL) for UDG, the relative standard deviations (RSDs) of peak time and peak area for different analytes were as follows: 2.50%-4.37% and 3.24%-7.18% (inter-day); 1.37%-2.71% and 1.43%-3.02% (intra-day), 4.28%-6.08% and 4.16%-7.57% (column to column), respectively. And it can identify the inhibitor-like drugs, evaluate enzymatic kinetics and achieve the detection of three enzymes in cell extracts, providing a simple and powerful platform for simultaneous detection of more DNA repair enzymes.

Molecular Characterization and Antibiotic sensitivity of Staphylococcus sp. Isolated from Animal Skin wounds

A wide variety of commensal microorganisms reside on the skin, many of which secrete proteolytic enzymes that might have detrimental effects following an injury. These bacteria are considered opportunistic pathogens. The objective of the study is to isolate Staphylococcus sp. from animal skin and conduct molecular characterization of the recovered strains in order to examine their enzymatic production capabilities. The objective is to assess the antibiotic susceptibility of Staphylococcus sp. and determine the ideal conditions for bacterial development. A total of 25 swab samples were obtained from animal skin wounds in AL-Shatrah city. Each sample was cultured on nutrient agar, blood agar, and Mannitol salt agar (with a 7.5% NaCl concentration) as a specialized medium. All isolates underwent molecular diagnosis using the PCR technique. Additionally, 10 isolates were selected for sequencing using the Sanger dideoxy 16S rRNA sequencing method. Enzyme production properties were analyzed, and the sensitivity of bacteria to six antibiotics was studied. Additionally, the researchers investigated the ideal circumstances for bacterial proliferation. Analysis of 25 swab samples taken from animal skin wounds yielded a total of 18 isolates. Based on biochemical tests, the majority of these isolates were identified as Staphylococcus aureus, Staphylococcus haemolyticus, Staphylococcus epidermidis, and Staphylococcus borealis. Staphylococcus warneri and Staphylococcus epidermidis exhibited sensitivity to Novobiocin, with inhibition zones of 22mm and 21mm respectively. However, all other isolates that were examined showed resistance to novobiocin.

Comprehensive insight into recent algal enzymes production and purification advances: Toward effective commercial applications: A review.

Algal enzymes are essential catalysts in numerous biological reactions and industrial processes owing to their adaptability and potency. The marketing of algal enzymes has recently risen due to various reasons, including the cost-efficient manner of their cultivation in photobioreactors, the eco-friendly production of high biomass contents, sources of novel enzymes that used in many sectors (biofuel and bioremediation applications), sustainability, and more renewability. Oxidoreductases and hydrolytic enzymes are among the important applied algal enzymes in industrial applications, with annually growing demand. These algal enzymes have opened up new avenues for significant health advantages in reducing and treating oxidative stress, cardiovascular illness, tumors, microbial infections, and viral outbreaks. Despite their promising uses, commercial applications of algal enzymes face many difficulties, such as stability, toxicity, and lower data availability on specific and adequate catalytic mechanisms. Therefore, this review focuses on the algal enzyme types, their uses and advantages over other microbial enzymes, downstream and upstream processing, their commercial and marketing, and their challenges. With the constant development of novel enzymes and their uses, enzyme technology provides exciting options for several industrial sectors.

Edukasi Pengelolaan Sampah Berbasis Eco enzyme untuk Mengurangi Dampak Pencemaran Lingkungan dan Resiko ISPA di Desa Karangdiyeng Kabupaten Mokokerto

Waste management issues and its environmental and health impacts, particularly Acute Respiratory Infections (ARI), are significant concerns in Desa Karangdiyeng, Kabupaten Mojokerto. A large portion of the community still practices waste burning, which harms both the health and the environment. This community service activity aimed to increase public awareness of environmental pollution risks from waste burning and provide training on creating eco enzymes as an eco-friendly waste management solution. The methods used included seminars on environmental pollution and ARI, as well as practical eco enzyme production training. Results showed a significant improvement in community knowledge, with an average pretest score increasing by 47.5% after attending the seminar and training. Participants were also able to practice making eco enzymes and were given plant seedlings to utilize the eco enzyme as fertilizer. This activity successfully provided benefits by raising awareness of proper waste management and its health impacts, as well as offering practical skills in eco enzyme-based waste management.