Detergent Industry Research Articles

Optimization of Effluents Using Artificial Neural Network and Support Vector Regression in Detergent Industrial Wastewater Treatment

The freshwater is a challenge as the world’s population grows. The largest sources of water in this planet are brackish water and sea water. So, water purification process is very important during this water crisis using desalination and various water treatment techniques. In this paper, we have developed some machine learning approaches for a detergent industry in India. The whole effluent and waste disposal in the detergent industry were treated by different treatment process like air flotation, chemical coagulation, sedimentation and biological treatment through completely mixed activated sludge process. The soft computing techniques (i) a five-layered feed forward ANN (ii) a five-layered cascade forward neural network and (iii) support vector regression have been applied to optimize the proposed models. Training function are considered as Feed-Forward BP(MLP), Cascade Forward BP and SVR where as Training algorithm Levenberg Marquardt and Sequential minimal optimization have been used. Graphical representation has been given for different types of pollutants, effluent treatment plant flow, and Change of color of wastewater after treatment and mathematical operations for Mechanism on Support Vector Regression has been established. To get the best number of neurons for the hidden layer, the network was trained for varied numbers of iterations (Nbest). The data was statistically examined as well. The Nbest value was found to be 10, with the lowest root mean square error (0.066), mean square error (0.0043), and greatest R2 value (0.996); these values show that the predicted and experimental responses are similar, and plant performance was adequately predicted using the backpropagation ANN model thus ANN may be used to describe the process.

Overproduction of a thermo-stable halo-alkaline protease on agro-waste-based optimized medium through alternate combinatorial random mutagenesis of Stenotrophomonas acidaminiphila

A strain of Stenotrophomonas acidaminiphila, isolated from fermenting bean-processing wastewater, produced alkaline protease in pretreated cassava waste-stream, but with low yield. Strain improvement by alternate combinatorial random mutagenesis and bioprocess optimization using comparative statistical and neural network methods enhanced yield by 17.8-fold in mutant kGy-04-UV-25. Kinetics of production by selected mutant modeled by logistic and modified Gompertz functions revealed higher specific growth rate in mutant than in the parent strain, likewise volumetric and specific productivities. Purification by PEG/Na+ citrate aqueous two-phase system recovered 73.87% yield and 52.55-fold of protease. Its activity was stable at 5–35% NaCl, 45–75°C, and was significantly enhanced by 1–15 mM sodium dodecyl sulfate (SDS). The protease was inhibited by low concentrations of phenyl-methyl-sulfonyl fluoride but was activated by 1–5 mM Mn2+ suggesting a manganese-dependent serine‑protease. The 45.7 kDa thermo-halo-stable alkaline protease demonstrated keratinolytic and blood-stain removal potentials showing prospects in textile and detergent industries, respectively.

Purification, characterization and potential detergent industry application of a thermostable α-amylase from Bacillus licheniformis RA31

α-Amylase is an endoamylase catalysing the degradation of starch into maltose, maltotriose and glucose. The enzyme isolated from microbial sources possess unique properties of thermostability thus making it a useful tool in the detergent industry. Here, we explored a strain of thermophilic bacteria Bacillus licheniformis for its potential application in detergent industry. The B. licheniformis RA31 was isolated from soil samples of hot spring in Rampur district of Himachal Pradesh, India and grown on optimized media to produce thermostable α-amylase. The enzyme was ethanol precipitated, purified (12.93 fold, 55.52% yield and 621.93 U/mg specific activity) to homogeneity with a single band on SDS-PAGE (66 kDa) and native-PAGE (68 kDa). Purified enzyme displayed best activity in pH 8 buffer and 80% activity was retained in pH 7 and 10. It showed temperature optima at 70°C. Its activity was decreased at 70°C (70% after 4 h), 80°C (65% after 4 h) and 90°C (50% after 1 h). The enzyme was stimulated (126%; 5 mM) by barium chloride. It was relatively stable in the presence of commercial detergents (109-125%), SDS (84%), Tween 20 (88%), EDTA (72%) and β-ME (70% at 10 mM). Km and Vmax for the enzymatic hydrolysis of starch were 0.339 mg/mL and 1.450 mg/min, respectively. The enzyme revealed the highest specificity towards wheat starch granule (140% after 1 h) and SEM analysis displayed its biodegradation (2-10 h). Improved cleaning efficiency of potato curry stained fine cotton clothes were observed with enzyme assisted detergent advance treatment (0.02% w/v). The enzyme showed potential applications in detergent industry.

Pengaruh Citra Merek, Kualitas Produk Dan Persepsi Hargaterhadap Minat Beli Konsumen Deterjen Attack

Marketing in modern times is no longer focused on how the product sells, but there are many factors and strategies that companies must have. The development of the detergent industry in Indonesia is growing very rapidly. Evidenced by the number of circulating various brands. Detergent is one of the industrial products that is very important in everyday life, especially for household and industrial purposes. Detergents can be in the form of liquid, paste, or powder containing constituents of the active ingredients on the surface and constituents of additives. The purposes of this study are (1) to determine and analyze the effect of brand image on consumer buying interest, (2) to determine and analyze the effect of product quality on consumer buying interest, (3) to determine and analyze the effect of price perception on consumer buying interest ( 4) To find out and analyze the effect of Brand Image, Product Quality and Price Perception together on Consumer Buying Interest. The number of respondents in this study found 100 respondents who were taken from housewives in the city of Bogor. The research data was processed using SPSS. The results of this study are as follows: (1) Brand Image has a positive and significant effect on Buying Interest in Attack detergent products with a regression coefficient value of 0.340 and a significant value of 0.028. (2) Product quality has a positive and significant effect on Buying Interest in Attack detergent products with a regression coefficient value of 0.272 and a significant value of 0.029. (3) Price Perception has a positive and significant effect on Buying Interest on Attack detergent products with a regression coefficient value of 0.325 and a significant value of 0.012. (4) Brand Image, Product Quality and Price Perception together have a positive and significant effect on Purchase Interest in Attack detergent products with a calculated F value of 28.912 and greater than the F table of 2.70 and has a significance value of 0.000.
 
 
 
 
 
 
 
 Keywords: Brand Image, Product Quality, Price Perception and Consumer Buying Interest

A Review on Versatile Eco-Friendly Applications of Microbial Proteases in Biomedical and Industrial Applications

Enzymes are the keystone for metabolism or the chemical reactions in biological systems. They help to build certain substances and break others down. Enzymes play a critical role in our bodies, industries and corporate sectors. Protease is an enzyme that helps break the peptide bonds present in the protein and separates the amino acids. Microbial proteases are the ones where the bacteria can produce the protease enzyme. Among many industrial enzymes, microbial protease has a versatile role in many fields like laundry, leather preparation, feather degradation, detergent preparation, biocontrol agents, optical lens cleaners, tannery, deproteinization of prawn shell, prevention of putrefaction of cutting oil, food preservatives, chelating agents, fodder additives, removal and degradation of polymeric substances (EPS), removal of hairs in buffalo hide, waste treatment, bioremediation process, reduction of waste-activated sludge and biofilm formation, degumming of silk, cosmetics (to remove glabellar-frown lines), cheese making, Meat tenderization, rehydration of goat skins and reduced water quantity, fibrin degradation, photographic, silver recovery from X-ray films, dairy industry, control harmful nematodes, fruit juice, and bakery, soybean paste, and sauce industry, pulp mills, alcohol production, fish processing wastes, prion degradation. Microbial protease is popularly used in the detergent industry, leather industry, textile industry, food industry, dairy industry, meat processing industry, bakery industry, pharmaceutical industry, etc.

Synthesis of Some Alkyl Polyglycosides

Surfactants are indisputably more important today, in terms of their use in industry and daily life, as well as the tasks they perform. In recent years, due to the driving force of environmental concerns, orientations to alternatives of surfactants that cause less or no harm to the environment have accelerated. One of these trends is the synthesis of alkyl polyglycosides (APG) and their use in the detergent industry. In this study, different acidic catalysts were used for the synthesis of APGs and the highest yield was achieved with sulfuric acid. APGs with different carbon numbers were obtained using octanol, decanol, dodecanol, and octanol/cetyl alcohol (w/w 80/20). The FTIR spectra of the structures of APG products obtained with these fatty alcohols and some commercial APG products were compared, and their structures were elucidated. In addition, the foam quality of the obtained APGs and the hydrophilicity properties they impart to the textile material were compared with some commercial surfactants, and the results were interpreted and evaluated.

Statistical Approach to Enhance α-Amylase Production from Bacillus licheniformis and Purification of the Enzyme

Background: The most widely used thermostable enzymes are the amylases in the starch industry. These are among the most important enzymes and are of great significance in present day biotechnology. Objective: The main objective of the present study was to enhance α-amylase production from Bacillus licheniformis using Response Surface Methodology (RSM) and the purification of the enzyme to homogeneity. Method: Bacterial culture producing α-amylase isolated from hot spring (Himachal Pradesh) was identified as Bacillus licheniformis using 16S rDNA gene sequencing (NCBI Accession No.: KR340466). Medium components and physical culture parameters viz. pH, temperature, inoculum size, peptone concentration and starch concentration were optimized using RSM. Among these five factors, three factors (starch concentration, peptone concentration and inoculum size) had a positive effect on amylase production. A 4.09-fold increase in the production of α-amylase from B. licheniformis was achieved using RSM as compared to One Factor At a Time. The enzyme was purified by using Diethylaminoethyl Cellulose column chromatography and subsequently by Sephadex G-75 gel filtration chromatography. Result: A purification fold of 23.39 and a yield of 12.12% were observed. A single band of 33 kDa was obtained using Sodium Dodecyl Sulphate (SDS) and native-Poly Acrylamide Gel Electrophoresis (PAGE), which indicated that the enzyme was purified to homogeneity and was a monomer. The enzyme showed stability at 50 and 65°C temperatures and at alkaline pH. Conclusion: The stability of purified enzyme at high temperatures and alkaline pH suggested its wide application in textile, detergent and paper industries.

Enhancing Lipase Production of Bacillus salmalaya Strain 139SI Using Different Carbon Sources and Surfactants

Microbial lipase is one of the major sources of the enzyme that has been broadly exploited in the food, detergent, and pharmaceutical industries due to its high catalytic activity, high yield, and environmental friendliness and cost-effectiveness. Therefore, the aim of this study was to optimize the medium for the submerged fermentation for lipase production by a novel strain, Bacillus salmalaya strain 139SI. The media subjected to lipase production was Luria Bertani (LB) with different carbon sources and surfactants supplemented to determine which would give the highest lipase activity of Bacillus salmalaya. The Lipase activity of the supernatant containing lipase enzyme was ddetermined using the titrimetric method with hydrolysis reaction. Results showed that the olive oil that was used as a carbon source, induced the highest lipase activity (11.0 U/mL) compared to sunflower oil (9.6 U/mL) and cooking oil waste (7.8 U/mL). For surfactants, LB medium supplemented with tween 80 enhanced higher lipase activity (6.8 U/mL) compared to tween 20 (6.0 U/mL) and sodium dodecyl sulphate (SDS) (2.0 U/mL). Thus, it can be concluded that submerged fermentation allows optimization of the culture medium whereby, among carbon sources, olive oil induced the highest lipase production, whereas Tween 80 was the best lipase inducer compared to other surfactants.

Biodegradation potential of sodium dodecyl sulphate (SDS) by mixed cells in domestic and non-domestic actual wastewaters: Experimental and kinetic studies

This study aimed to assess and compare the potential of sodium dodecyl sulfate (SDS) biodegradation in four types of real-field effluents including domestic wastewater (DWW), laundry wastewater (LWW), carwash garage wastewater (CWW), and wastewater from household detergent industry wastewater (HWW) using non adapted mixed cells having Pseudomonas medocina and Bacillus as the dominant types of bacterial cells. Examining and comparing various types of actual wastewaters supported the originality of this study by considering different levels of SDS concentrations, meanwhile, taking into account implicitly the effect of different species associated with SDS based on the origin of wastewater. The effect of inoculum size including 1%, 3%, 5%, 7%, and 10% (v/v) as well as the SDS initial concentrations of10, 20, 50, 100, 300, 500, and 1000 mg/L were explored. The results demonstrated that the removal efficiency of SDS in the DWW, LWW, CWW, and HWW were 99.63%, 92.31%, 98.78%, and 85.77%, respectively after 48 h. The outcomes of this study revealed the potential and significance of SDS removal in actual effluents by aerobic biodegradation regardless of its concentration. Haldane kinetics model fitted the experimental data very well compared to Monod and Han-Levenspiel models with determination coefficient (R2), sum square error (SSE), and P-value of 0.96, 1.65 × 10−14, and 1.57×10−5, respectively indicating the inhibitory action of SDS at high concentrations.

Stain removing, juice-clarifying, and starch-liquefying potentials of amylase from Pleurotus tuberregium in submerged fermentation system

BackgroundAmylase is used commercially in food, textiles, sugar syrup, paper, and detergent industries. Bacteria and fungi remain a significant source of industrial enzymes. Pleurotus tuberregium is a macro-fungi that can exist as a fruiting body, sclerotium, mycelium, and spores. Some studies have been conducted on this fungus, with minimal studies on its enzyme activity (s) using the submerged fermentation technique. ResultsThe purified amylase has a specific activity of 5.26 U/mg, total activity of 189.20 U, maximally active at 70 °C, pH of 5, and retaining 100% of its activity at 30 oC for 4 min. P. tuberregium amylase showed optimal activity with plantain peel, followed by starch and pineapple peel (42, 30, and 29 μg/mL/min respectively). The presence of Ca2+, Mg2+, and Na+ ions in the reaction mixture activated the enzyme activity, but was slightly and moderately inhibited by KCl and Na2H2PO4 respectively. The crude enzyme effectively clarified juice, liquefied soluble cassava starch (with a release of appreciable glucose quantity), and partially de-stained white fabric. ConclusionsThe amylase obtained from the submerged fermentation of Pleurotus tuberregium has potential applications in food and detergent industries.

Biodegradation of hazardous naphthalene and cleaner production of rhamnolipids — Green approaches of pollution mitigation

Toxic and hazardous waste poses a serious threat to human health and the environment. Green remediation technologies are required to manage such waste materials, which is a demanding and difficult task. Here, effort was made to explore the role of Pseudomonas aeruginosa SR17 in alleviating naphthalene via catabolism and simultaneously producing biosurfactant. The results showed up to 89.2% naphthalene degradation at 35 °C and pH 7. The GC/MS analysis revealed the generation of naphthalene degradation intermediates. Biosurfactant production led to the reduction of surface tension of the culture medium to 34.5 mN/m. The biosurfactant was further characterized as rhamnolipids. LC-MS of the column purified biosurfactant revealed the presence of both mono and di rhamnolipid congeners. Rhamnolipid find tremendous application in medical field and as well as in detergent industry and since they are of biological origin, they can be used as favorable alternative against their chemical counterparts. The study demonstrated that catabolism of naphthalene and concurrent formation of rhamnolipid can result in a dual activity process, namely environmental cleanup and production of a valuable microbial metabolite. Additionally, the present-day application of rhamnolipids is highlighted.

Expression and characterization of a family 45 glycosyl hydrolase from Fomitopsis pinicola and comparison to Phanerochaete chrysosporium Cel45A

To efficiently decompose biomass, fungi have developed various enzymatic and non-enzymatic strategies and are a source of versatile biocatalysts. The endoglucanases in glycosyl hydrolase CAZy family 45 (GH45) are known for their small size, a high thermostability and a broad substrate specificity that has been employed in textile and detergent industries. Here we report the heterologous expression and characterisation of an GH45 endoglucanase from the brown rot Fomitopsis pinicola and its direct comparison to an already characterised GH45 from the white rot Phanerochaete chrysosporium. Both enzymes were recombinantly expressed in Pichia pastoris and purified by two chromatographic steps. The biochemical characterisation highlighted the acidophilic character, with an optimal pH of 4, and a preference for amorphous substrates as carboxymethyl cellulose (CMC) and substrates containing β-1,4-glucans rather than the previously reported β-1,3/1,4-glucans lichenan and β-glucan. The dominating products from β-1,4-glucans were C3–C6 oligosaccharides, whereas from β-1,3/1,4-glucans glucose was the main reaction product. From the characterisation no differences between the brown rot and the white rot GH45 was evident.

Screening and optimization of candidate alkaline protease for dehairing potential from marine Bacillus paramycoides M2

Alkaline proteases are active from neutral to alkaline pH range and have extensive applications in detergent and leather industries. In the present research, bacteria isolated from marine water samples were screened for proteolytic activity. Among the isolates, M2 showed maximum proteolysis with a clear zone when cultured on skim milk agar plates at 37°C for 24 h. Molecular identification using 16S rRNA sequencing and phylogenetic analysis revealed that M2 has sequence identity (99.93%) to Bacillus paramycoides. SEM analysis was carried for determining the morphology of M2 and also for enzyme treated skin. FAME analysis using GCMS was performed for the determination of fatty acids in the strain. The selected isolate was inoculated into protease production medium under submerged fermentation conditions at 37ºC for 48 h with a constant agitation of 120 rpm. Protease activity was determined under varying conditions of pH, incubation temperature, carbon and nitrogen sources, metal ions and NaCl (1- 5%) using casein as substrate. The isolate M2 utilized molasses and peptone as carbon and nitrogen sources for better alkaline protease production at 40°C and pH 10 under optimal conditions. The dehairing experiments with M2 alkaline protease revealed dehairing efficacy of protease over chemical treatment. Hence, extracellular alkaline protease from M2 isolate could find potential application in leather processing industries and can be exploited commercially.

Structural and functional adaptation in extremophilic microbial α-amylases.

Maintaining stable native conformation of a protein under a given ecological condition is the prerequisite for survival of organisms. Extremophilic bacteria and archaea have evolved to adapt under extreme conditions of temperature, pH, salt, and pressure. Molecular adaptations of proteins under these conditions are essential for their survival. These organisms have the capability to maintain stable, native conformations of proteins under extreme conditions. The enzymes produced by the extremophiles are also known as extremozyme, which are used in several industries. Stability and functionality of extremozymes under varying temperature, pH, and solvent conditions are the most desirable requirement of industry. α-Amylase is one of the most important enzymes used in food, pharmaceutical, textile, and detergent industries. This enzyme is produced by diverse microorganisms including various extremophiles. Therefore, understanding its stability is important from fundamental as well as an applied point of view. Each class of extremophiles has a distinctive set of dominant non-covalent interactions which are important for their stability. Static information obtained by comparative analysis of amino acid sequence and atomic resolution structure provides information on the prevalence of particular amino acids or a group of non-covalent interactions. Protein folding studies give the information about thermodynamic and kinetic stability in order to understand dynamic aspect of molecular adaptations. In this review, we have summarized information on amino acid sequence, structure, stability, and adaptability of α-amylases from different classes of extremophiles.

The changing face of SDS denaturation: Complexes of Thermomyces lanuginosus lipase with SDS at pH 4.0, 6.0 and 8.0

HypothesisLipases are widely used in the detergent industry and must withstand harsh conditions involving both anionic and zwitterionic surfactants at alkaline pH. Thermomyces lanuginosus lipase (TlL) is often used and stays active at high concentrations of the anionic surfactant sodium dodecyl sulfate (SDS) at pH 8.0, but is sensitive to SDS at pH 6.0 and below. We propose that enhanced stability at pH 8.0 results from a structurally distinct complex formation with SDS. ExperimentsWe use small-angle X-ray scattering (SAXS) to elucidate structures of TlL:SDS at pH 4.0, 6.0, and 8.0 and further investigate the complexes at pH 8.0 using hydrogen/deuterium exchange mass spectrometry (HDX-MS). FindingsAt pH 4.0, large dense aggregates are formed at low [SDS], which become gradually less dense at higher [SDS], resulting in a core–shell structure. At pH 6.0, SDS induces a TlL dimer and forms a hemi-micelle along the side of the dimer. At higher [SDS], TlL adopts a core–shell structure. At pH 8.0, TlL forms a dimer with a SDS hemi-micelle but avoids a core–shell structure and maintains activity. Three helices are identified as SDS anchor points. This study provides important structural insight into the stability of TlL towards SDS under alkaline conditions.

Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene from Bacillus thuringiensis for detergent industry.

Present study was aimed to clone and express the esterase encoding gene from Bacillus thuringiensis in E. coli BL21. Purification of recombinant esterase enzyme was achieved up to 48.6 purification folds by ion exchange chromatography with specific activity of 126.36 U mg-1. Molecular weight of esterase enzyme was 29 kDa as measured by SDS-PAGE. Purified esterase enzyme showed stability up to 90% at 90 °C and remained stable in a wide pH range (8-11). Molecular docking strengthens the experimental results by showing the higher binding energy with p-NP-butyrate. Enzyme activity was found to be reduced by EDTA but enhanced in the presence of other metal ions. Enzyme activity was reduced with 1% SDS, PMSF, and urea but organic solvents did not show considerable impact on it even at higher concentrations. Purified recombinant esterase was also found to be compatible with commercial laundry detergents and showed very good stability (up to 90%). All these properties proved the esterase enzyme from B. thuringensis a significant addition in detergent industry.

Microbial Enzymes and Their Applications in Food Industry: A Mini-Review

The use of enzymes is replacing chemicals in many industrial production processes because of the eco-friendly nature of enzymes which do not generate greenhouse gases and have reduced the demand for energy in industries. To meet the ever-increasing demand for enzymes in many industries and survive the harsh production conditions, microbial sources of enzyme production are the most preferred source for industrial enzyme production because the microbes are readily available, they grow at a very fast rate, and they can be genetically manipulated to produce enzymes which can perform optimally at different industrial production conditions. Microbial enzymes have found so many applications in various industries (textiles, leather, paper and pulp, research and development, pharmaceutical, agriculture, detergent, waste, biorefineries, photography and food industries), thus making them very essential in several industrial production processes. Here in this review, the application of some important microbial enzymes in food industry and the microbial sources for the enzymes are discussed.

Review of Strategies for the Industrial Production of α-amylase by Bacillus subtilis

Bacillus subtilis can secrete industrially important proteins such as proteases and α-amylases and used on industrial scale. α-Amylase enzyme has market demands due to its applications in food, bakery, detergent industries, starch liquefaction, pre-digestion of the animal feed to enhance its quality, sizing of the fibres in textiles. The safety issues associated with the use of this bacteria for industrial applications are studied and it has been observed that the products obtained from it are having GRAS status of US Food and Drug Administration. Bacillus subtilis is considered the most widely experimental organism to conduct the genetic modification studies due to its properties which make it a suitable host for biosynthesis of the products. The genomic structure of Bacillus subtilis can be modified with the help of high quality genomic sequences. The genetic strategies for such modifications include the use of mutagenic treatments, screening of better expression systems, use of better promoters and high secretion level peptides. Another aspect of these strategies to enhance the enzyme yield includes the application of different fermentation methods and use of different substrates. Present review article summarizes some of such strategies applied for obtaining higher yields of α-amylase enzyme using Bacillus subtilis.

Foaming Characteristics of Saponins of Leaves of Hibiscus Sabdariffa Linn (Red Variety)

The aim of this study was to determine the foaming characteristics (foam power and foam stability) of saponins of the leaves of Hibiscus sabdariffa Linn. The preliminary screening for saponins and phytochemical screening were carried out to determine the probable presence of saponins and other secondary metabolites. The results showed the probable presence of saponins in the leaves of Hibiscus sabdariffa Linn. Cold maceration extraction method was conducted and yields were obtained from the extracts i.e. aqueous, methanol, and n-butanol. The methanol extract possessed the highest yield of 46.53 % compared to aqueous and n-butanol extracts with 8.15 % and 0.69 % respectively. The foam heights and foaming times of aqueous, methanol and n-butanol extract and that of synthetic detergents (Tween 80 and Triton X-100) when subjected to statistical analysis (ANOVA) showed significant decreases (at p<0.05) between the foam heights (H 0, H 1, and H 5 ) and foaming times (Tc) at varying concentrations. The foam power of n-butanol extract at 0.5 % was the highest with values of 40.47 % indicating that it was not stable when compared with the values of 87.28 % and 73.57 % for Triton X-100 and Tween 80 respectively. Therefore, saponins of the leaves of Hibiscus sabdariffa Linn. may be of limited use in the detergent industries but relevant in related industries. It is recommended that the foaming properties of the crude saponins would be more enhanced when subjected to further purification processes to meet the standards of Triton X-100 and Tween 80.

Efficiency and Determinants of Capital Structure in the Greek Pharmaceutical, Cosmetic and Detergent Industries

The purpose of this paper is to investigate the relationship between a firm’s capital structure (i.e., leverage) and its operating environment, taking into account firm (i.e., efficiency, asset structure, profitability, size, age and risk) and industry effects. For a sample of Greek pharmaceutical, cosmetic and detergent (PCD) enterprises, firm efficiency was estimated using bootstrapped data envelopment analysis (DEA), and a leverage model was produced using ordinary least squares (OLS) regression. The findings confirm the significance of firm efficiency (i.e., the franchise-value hypothesis over the efficiency-risk hypothesis) and asset structure on leverage. Efficiency and overall and short-term leverage have a significant negative relationship, indicating that more efficient firms tend to choose a relatively low debt ratio. Pharma firms are more affected since they are less efficient than cosmetics and detergents firms. Furthermore, asset structure and short- and long- term leverage have a significant negative and positive relationship, respectively, indicating that the firms with more tangible assets have less short-term debt and more long-term debt in their capital structure. Cosmetic and detergent firms, which have slightly more tangible assets than pharma firms, appear to be able to substitute high-cost, short-term debt with the low-cost, long-term debt by using such assets as collateral.