Washing Performance Research Articles

Optimization and purification of a novel calcium-independent thermostable, α-amylase produced by Bacillus licheniformis UDS-5.

Microbial amylases should essentially remain active at higher temperatures, and in the alkaline pH and a range of surfactants to be suitable as detergent additives. In the present study, a thermophilic amylase producing bacterium, Bacillus licheniformis UDS-5 was isolated from Unai hot water spring in Gujarat, India. It was identified as a potent amylase producer during starch plate-based screening process. Therefore, the physicochemical parameters influencing amylase production were optimized using Plackett-Burman design and Central Composite Design. The amylase was purified through ammonium sulfate precipitation, size exclusion and ion exchange chromatography, achieving the purification fold and yield to be 9.2 and 40.6%, respectively. The enzyme displayed robust stability and activity across a wide range of temperatures and pHs, with an increased half-life and reduced deactivation rate constant. The amylase exhibited optimal catalysis at 70°C and pH 8. The kinetic studies revealed Km and Vmax values of 0.58mg/mL and 2528μmol/mL/min, respectively. Besides, the purified amylase displayed stability in the presence of various metal ions, surfactants, and chelators suggesting its potential for industrial applications, particularly in the detergent industry. Moreover, detergent application studies demonstrated its efficacy in enhancing washing performance. A comparative profile on washing efficiency of the studied amylase and the commercial amylase with various detergents pointed towards its possible future use as a detergent additive.

Pengungkapan Kinerja Lingkungan Instansi Pemerintah Daerah Melalui Laporan Keberlanjutan Berbasis Global Reporting Initiative

Laundry washing is a crucial process in daily life. Although automatic washing machines have simplified the washing process, utilizing advanced technology like fuzzy logic control can enhance the performance of smart washing machines to achieve optimal washing results. This research aims to implement fuzzy logic control using the Mamdani method on smart washing machines to improve efficiency and washing quality. The research methodology consists of several stages. Firstly, analyzing variables that affect the washing process, such as laundry load, fabric thickness, dirt level, and water temperature. Next, designing a Mamdani fuzzy logic control system by determining membership functions for each variable and creating fuzzy rules to link input and output variables. Lastly, evaluating washing results based on predefined input variables. The research findings demonstrate that implementing Mamdani fuzzy logic control on smart washing machines can significantly enhance washing quality and adaptively determine washing parameters to achieve cleaner washing outcomes. Therefore, integrating Mamdani fuzzy logic control into smart washing machines has the potential to improve overall washing performance. In conclusion, utilizing Mamdani fuzzy logic control on smart washing machines is an effective step towards enhancing efficiency and effectiveness in laundry washing. This research contributes to the development of more adaptive and environmentally-friendly smart washing machine technology and plays a crucial role in advancing fuzzy logic control technology for other smart household applications.

A lipase from Lacticaseibacillus rhamnosus IDCC 3201 with thermostability and pH resistance for use as a detergent additive

Lipases are important biocatalysts and ubiquitous in plants, animals, and microorganisms. The high growth rates of microorganisms with low production costs have enabled the wide application of microbial lipases in detergent, food, and cosmetic industries. Herein, a novel lipase from Lacticaseibacillus rhamnosus IDCC 3201 (Lac-Rh) was isolated and its activity analyzed under a range of reaction conditions to evaluate its potential industrial application. The isolated Lac-Rh showed a molecular weight of 24 kDa and a maximum activity of 3438.5 ± 1.8 U/mg protein at 60 °C and pH 8. Additionally, Lac-Rh retained activity in alkaline conditions and in 10% v/v concentrations of organic solvents, including glycerol and acetone. Interestingly, after pre-incubation in the presence of multiple commercial detergents, Lac-Rh maintained over 80% of its activity and the stains from cotton were successfully removed under a simulated laundry setting. Overall, the purified lipase from L. rhamnosus IDCC 3201 has potential for use as a detergent in industrial applications.Key points• A novel lipase (Lac-Rh) was isolated from Lacticaseibacillus rhamnosus IDCC 3201• Purified Lac-Rh exhibited its highest activity at a temperature of 60 °C and a pH of 8, respectively• Lac-Rh remains stable in commercial laundry detergent and enhances washing performance

Exploration of a novel protease from Phytolacca dodecandra (Endod) berries for potential application in detergent formulation

AbstractConventional detergent formulations contain either petroleum‐derived or synthetic chemicals. Hence, the replacement of these chemicals with natural products such as enzymes is considered a green technology. Among these enzymes, protease is renowned in detergent formulations. Therefore, the objective of this study was to explore and characterize a new protease from Phytolacca dodecandra, because the plant is traditionally known for detergency purposes. Enzyme extraction was performed with Glycine/NaOH buffer, pH = 10.0. Gelatin hydrolysis and agar well diffusion tests were implemented as qualitative assays, whereas the enzyme assay technique was applied for the quantitative investigation of the new protease from plant extracts. The crude enzyme was partially characterized concerning temperature and pH tolerance, washing performance, detergent compatibility, and stability. The finding of this study revealed that Phytolacca dodecandra contains protease and is characterized by 1418.84 U/mL of enzyme activity, where 1 unit (U) of enzyme activity refers to the amount of enzyme required to liberate 1 μg of tyrosine/mL/min under the defined assay conditions. The enzyme showed maximum activity at pH 10.5 and 45°C. The enzyme was stable and maintained 99.52% activity at 40°C and 91.73% at pH 10.0 after 2 h pre‐incubation. The enzyme showed excellent wash performance and could potentially remove blood stains completely within 3 min. After 2 h of pre‐incubation the enzyme maintained 69.06% and 54.88% of its activity in the presence of Azzy and Sunlight, respectively. The enzyme maintained 71.99% of its residual activity after 60 days of storage. If further studies are conducted, all these properties of the newly investigated protease can make the enzyme applicable in detergent formulations.

Enhancing Antibacterial and Water-Repellent Properties for the Production of High-Performance Fabrics in Home Textiles

In this research, we aimed to enhance the antibacterial activity and water repellency functionalities of single-layer 100% cotton fabrics on both the face and back sides, utilizing conventional methods. Unlike conventional approaches that often rely on lamination or coating techniques to imbue fabric surfaces with distinct properties, our study pursued a cost-effective strategy using traditional textile finishing methods. By integrating double functionality into cotton fabric, we aimed to circumvent the need for additional equipment and high initial costs associated with other techniques. To achieve this, we improved the antibacterial activity of the fabrics through the incorporation of silver ions in the pad-dry process. Simultaneously, water repellency functionality was introduced through a printing application, where the printing paste, devoid of dyestuff, was combined with functional agents and applied using rotary printing to the fabric’s backside. Following these finishing applications, we conducted comprehensive tests encompassing washing durability, antibacterial efficacy, water repellency, mechanical strength, and fastness properties of the multifunctional fabrics. Characterization tests, including Fourier transform infrared attenuated total reflectance (FTIR-ATR) and scanning electron microscope analyses (SEM-EDX), were performed. The outcome of our study showcased the successful enhancement of double-functional cotton fabric, featuring water repellency and antibacterial efficiency on distinct sides. Furthermore, the results indicated that these functionalities endured up to 20 washing cycles, with fastness and performance tests consistently achieving peak levels.

Simple model for water wash performance in amine scrubbing for CO2 capture

In amine-based capture systems, a water wash is necessary to remove gaseous amine to minimize atmospheric emissions and maximize amine recovery. Water wash simulation requires rigorous thermodynamic and kinetic models like those for absorption and stripping systems. An offline water wash model has been developed based on simplified thermodynamic and mass transfer assumptions to simulate a single-stage water wash for flue gas from gas-fired turbines with little or no aerosol, and to expedite simulations without needing to utilize process modeling software. Calculation of activity coefficients using both Pitzer–Debye–Hückel and Debye–Hückel theory suggest that the liquid phase in a typical water wash will be ideal due to the dilute concentration of molecular and ionic species.Vapor phase piperazine (PZ) is predicted with a driving force based on the volatility of the free amine that has not reacted with other species or dissociated into its ionic form, and the predicted outlet concentration is nearly identical to that predicted by rigorous Aspen PlusⓇ simulations. The predicted UT FEED outlet concentration is 220 ppb compared to 260 ppb predicted by Aspen PlusⓇ.Single-stage water washes are predicted to have single ppm concentration of MEA leaving the wash outlet flue gas. Amino-methyl-propanol (AMP) is predicted to be reduced to 10–30 ppm by a single-stage wash, and is predicted to be a difficult-to-capture amine without further washing steps. This prediction correlates with published TCM data from an ALIGN-CCUS campaign. Amine compounds at a similar or lower volatility to that of PZ are predicted to be reduced to ppb levels via a single-stage wash.

Biovalorizing agro-waste ‘de-oiled rice bran’ for thermostable, alkalophilic and detergent stable α-amylase production with its application as laundry detergent additive and textile desizer

The current research was concerned with the use of abundant agro-waste ‘de-oiled rice bran (DORB)’ as a sustainable substrate to produce α-amylase followed by several targets like process parameter optimization for augmented production and immobilization. In addition, we have also focused on investigating the application of DORB_amy as an efficient laundry detergent additive and textile desizer. The best production was recorded at pH 8.0 at 37 °C after 96 h incubation with 1.5 % (w/v) maltose. The DORB_amy has optimum activity at pH 9.0 at 60 °C with a Km and Vmax of 0.31 mg/mL and 222.22 mg/mL/min respectively. The catalytic performance of DORB_amy was further enhanced after immobilization in 3.0 % calcium alginate beads with 61.95 ± 0.17 % of operational stability after five continuous reaction cycles. The findings showed excellent performance of DORB_amy in cleaning starchy stains. The washing performance of enzyme and detergent together was better than their individual performance which increases the application of α-amylase as a laundry detergent additive. About 17.34 % weight loss or desizing was done by DORB_amy with an 8–9 TEGEWA rating. The reported biochemical features like thermostability, alkalophilic and detergent-stable nature of the DORB_amy make it industrially fit with great significance.

Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test.

The potential of strawberry-derived protease as a component of laundry detergent is investigated. The compatibility of the enzyme with various surfactants, oxidizing agents, and commercial detergents is tested. The immobilized enzyme prepared by immobilizing Co2+ ions together with the enzyme is also tested. Strawberry crude protease shows high stability in the presence of surfactants frequently used in detergents. The enzyme is found to be relatively stable to oxidizing agents. In addition, it is determined that strawberry protease works in excellent compatibility with different commercial solid and liquid detergents in the Turkish market and also maintains its stability very well. Washing tests based on visual examination also reveal that the enzyme improves the washing performance of the tested detergent. All these properties and high activity at alkaline pH make this enzyme a very strong candidate for use in laundry detergent formulations.

Solvent degradation and emissions from a CO2 capture pilot at a waste-to-energy plant

Degradation and emissions of amine-containing solvents from CO2 capture plants are important to address as we are getting closer to full-scale deployment. Solvent degradation and air emissions from CO2 capture with 30 wt% monoethanolamine (MEA) were monitored at a mobile capture pilot, treating flue gas from a waste-to-energy facility in Denmark. The release of nitrosamines and nitramines was shown to be below the detection limit. Preliminary results showed that the installation of an acid wash removes gaseous degradation products from the depleted flue gas by up to 83% for MEA. However, a more in-depth investigation of the acid wash performance is needed to fully make any conclusions. The release of CO, NO, NO2, SO2, NH3, and HCl was monitored over several days. Results showed that the release of these components in the depleted flue gas is affected by both the temperature in the wash tower and the process configurations. The emissions of CO, NO, NO2, SO2, NH3 and HCl in the CO2 product stream were below 5 mg/m3. Heat stable salts accumulate over time in 30 wt% MEA with formate and acetate being the main degradation products. Accumulation of iron in the solvent did not exceed 10 mg/L during the 4 month campaign. The solvent degradation and emission results obtained in this study create a solid basis for understanding potential solvent emissions to the environment from waste-to-energy plants. Currently, the accumulation of heat stable salts in amine-based solvent seems to be the main challenge. SynopsisThese results are important to control solvent based emissions and waste products in CO2 capture technology.

Fungal Crude Lipase Enzyme Produced Using the SSF (Solid State Fermentation) Method Increases The Washing Test Performance

Lipase is an enzyme that commonly used in various industries, including the detergent industry to improve washing performance. Two fungal isolates (Al and Cl) has been reported to be highly active on high pH. This research aims to see the potential of those fungi (crude enzyme) in improving washing performance. Enzymes were produced using the SSF (Solid State Fermentation) method with sugarcane bagasse as a medium. To determine how adding enzymes might affect the effectiveness of washing, studies were conducted. The results show that washing performance increases from 52% (detergent only) to 74% in combination with the crude enzyme. It is concluded that Al has a potential to be involved in biodetergent production. Similar assays with concentrated enzymes are suggested for future studies.

Alkaline Thermo- and Oxidant-Stable Protease from Bacillus pumilus Strain TNP93: Laundry Detergent Formulations.

The study aims to produce a detergent-compatible and alkaline thermophilic protease from a Bacillus strain and to investigate its usability as a detergent bio-additive. The protease-producing bacterium was identified as Bacillus pumilus strain TNP93 according to the 16S rRNA sequence. The bacterium optimally synthesized the protease at 40°C and pH 10 in 40h. The raw protease displayed its optimum activity at pH 10 and 60°C and its stability between pH 6-13 and 30-100°C for 24h. The molecular mass of the proteolytic band was estimated to be about 85kDa. The protease was not inhibited by any of the metal ions used (Ba2+, Ca2+, Co2+, Cu2+, Mg2+, Mn2+, Zn2+). 97 and 90% of its original activity with 5mM PMSF and EDTA remained. The activity was measured as 84, 124, and 95%, respectively, in the presence of 1% concentrations of Tween 20, Tween 80, and Triton X-100. In addition, all of its activity was preserved when the enzyme was exposed to 5% H2O2. The end products of casein were detected as tyrosine, aspartic acid, glycine, and cysteine by thin-layer chromatography. Considering the wash performance analysis, the mix of 1% commercial detergent and enzyme almost removed all of the protein-based stains (blood and egg yolk albumin). These remarkable findings indicate that the alkaline, thermo-, and oxidant-stable TNP93 protease is a valuable candidate for usage as a biological additive in various laundry detergents.

Continuous On-Chip Cell Washing Using Viscoelastic Microfluidics.

Medium exchange of particles/cells to a clean buffer with a low background is essential for biological, chemical, and clinical research, which has been conventionally conducted using centrifugation. However, owing to critical limitations, such as possible cell loss and physical stimulation of cells, microfluidic techniques have been adopted for medium exchange. This study demonstrates a continuous on-chip washing process in a co-flow system using viscoelastic and Newtonian fluids. The co-flow system was constructed by adding a small amount of biocompatible polymer (xanthan gum, XG) to a sample containing particles or cells and introducing Newtonian fluids as sheath flows. Polymer concentration-dependent and particle size-dependent lateral migration of particles in the co-flow system were examined, and then the optimal concentration and the critical particle size for medium exchange were determined at the fixed total flow rate of 100 μL/min. For clinical applications, the continuous on-chip washing of white blood cells (WBCs) in lysed blood samples was demonstrated, and the washing performance was evaluated using a scanning spectrophotometer.

Asymmetric Multienergy-Coupled Radiative Warming Textiles for Personal Thermal-Moisture Management.

In order to address the requirements for warmth and energy conservation in cold climates, the development of personal thermal management textiles that regulate local human thermal comfort has emerged as a promising solution in recent times. Nevertheless, existing warming textile strategies often rely on a singular energy source, exhibit inadequate air/moisture permeability, and lack adaptability to dynamic and intricate climate variations. Herein, a novel multienergy-coupled radiative warming Janus textile has been effectively designed and fabricated via screen printing and foam finishing. Taking advantage of the synergistic effects of directional water transport capability of polyester-covered cotton (with a directional water-transport index of R = 577.5%), high mid-infrared radiant reflection (at 60%), electrothermal conversion of copper coating (with a sheet resistance of 0.01 Ω sq-1), and strong solar absorption of the nanoporous structure TA@APTES@Fe(III)@CNT (TAFC) coating (at 98.5%), the Janus fabric exhibits exceptional performance in expelling out one-way sweat/moisture (R = 329.3%) and solar heating (86.9 °C)/Joule heating (226.4 °C at 3.0 V)/heat retention (2.4 °C higher than that of cotton fabric). Furthermore, the fabric is also provided with exceptional mechanical, washing, flame-retardant, and antibacterial performance. This research holds the potential to revolutionize the development and production of warming textiles by incorporating desirable sweat/moisture permeability and multienergy-coupled heating.

Industrial washing conditions as factor that influence the cellulose structure and mechanical strength of bed linens

It is crucial for companies providing rental and maintenance services to hotels and hospitals to tackle the problem of decreased physical longevity caused by frequent laundering procedures in the industrial textile sector. Proper maintenance of bed linens is vital as they undergo multiple rigorous preservation techniques, such as being treated with chlorine to remove tough stains and sanitize the fabrics. The mechanical strength of fabric made of 100% cotton fibre products greatly relies on the degree of polymerization of cellulose-cotton fibre material. The study evaluated the washing performance of five cotton fabrics. Two weaving pattern variations were used and the fabrics were composed either of 100% cotton or a blend of 50% cotton and 50% polyester fibres. The washing methods included commercial and chlorine-based laboratory washing. 100% cotton fabrics, especially in plain weave show higher tensile strength falls then blended ones. The pure cotton fabric loss much more of its initial strength after only few chlorine-based washings than after hundred commercial ones. Limiting viscosity number values drop in half after hundred commercial washings for cotton fibres taken from tested woven fabrics. In comparison, decline of this parameter after only ten chlorine-based washings is more than 80% of their initial values. Performing the maintenance process without free chlorine, while still retaining its high effectiveness, can notably augment the frequency of maintenance procedures and preserve the mechanical durability of cotton fabrics over a longer time span. This leads to a reduction in textile waste residues.

Detergent-stable amylase production by Paenibacillus lactis strain OPSA3 isolated from soil; optimization by response surface methodology

This study aimed to isolate thermostable, alkaliphilic, and detergent-tolerant amylase-producing bacteria. Pure isolates from environmental samples were screened on a starch-based medium (pH 11), and selected isolates were identified using cultural and molecular techniques. Product optimization studies were conducted, and secreted amylase was partially purified using 40% (w/v) saturation ammonium sulfate at 4 °C. The wash performance of concentrated amylase was analyzed. A novel isolate, Paenibacillus lactis OPSA3, was selected for further studies. The isolate produced amylase optimally when grown on banana peels and soybean extracts, which are agro-wastes. Optimization by Response surface Methodology resulted in a 2.1-fold increase in alkaliphilic amylase production. A 2.46-fold purification was achieved, with an enzyme activity yield of 79.53% and specific activity of 26.19 Umg−1. Wash performance analysis using the amylase supplemented with boiled commercial detergent (kiln®) showed good cleaning efficiency. The amylase has the potential for application as a component of green detergent.

Magnetic Beads inside Droplets for Agitation and Splitting Manipulation by Utilizing a Magnetically Actuated Platform.

We successfully developed a platform for the magnetic manipulation of droplets containing magnetic beads and examined the washing behaviors of the droplets, including droplet transportation, magnetic bead agitation inside droplets, and separation from parent droplets. Magnetic field gradients were produced with two layers of 6 × 1 planar coils fabricated by using printed circuit board technology. We performed theoretical analyses to understand the characteristics of the coils and successfully predicted the magnetic field and thermal temperature of a single coil. We then investigated experimentally the agitation and splitting kinetics of the magnetic beads inside droplets and experimentally observed the washing performance in different neck-shaped gaps. The performance of the washing process was evaluated by measuring both the particle loss ratio and the optical density. The findings of this work will be used to design a magnetic-actuated droplet platform, which will separate magnetic beads from their parent droplets and enhance washing performance. We hope that this study will provide digital microfluidics for application in point-of-care testing. The developed microchip will be of great benefit for genetic analysis and infectious disease detection in the future.

The synthesis of calcium and barium salts of carboxymethylamine-methylalkylphenol and their effect on properties of ДС -11 engine oil

The authors suggest a simple environmental-friendly method to obtain the additives with anticorrosion and washing properties. Described method is based on the interaction of hydroxides of the alkaline-earth metals with carboxymethylamine-methylalkylphenol obtained via the reaction of the industrial alkylphenol with formaldehyde and the aminoacetic acid. The effect of synthesized compounds – calcium and barium salts of carboxymethylamine-methylalkylphenol on the anticorrosion and washing properties of ДС -11 oil has been studied. It was established that they show high anticorrosion and washing performance. In 2.5% concentration of the additive, the corrosion of ДС -11oil is eliminated. The compounds studied do not worsen other properties including the viscosity index and freezing temperature of studied ДС -11 oil. It was revealed that the composition from barium salts of carboxymethylamine-methylalkylphenol and ИХП-21 additive shows high anticorrosion, antioxidation and washing properties as well.

Biochemical characterization of an alkaline and detergent-stable Lipase from Fusarium annulatum Bugnicourt strain CBS associated with olive tree dieback.

This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A1 (PLA1) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulphate precipitation, Superdex® 200 Increase gel filtration and Q-Sepharose Fast Flow columns, with a total yield of 21%. The specific activity of FAL was found to be 3500 U/mg at pH 9 and 40°C and 5000 U/mg at pH 11 and 45°C, on emulsions of triocanoin and egg yolk phosphatidylcholine, respectively. SDS-PAGE and zymography analysis estimated the molecular weight of FAL to be 33 kDa. FAL was shown to be a PLA1 with a regioselectivity to the sn-1 position of surface-coated phospholipids esterified with α-eleostearic acid. FAL is a serine enzyme since its activity on triglycerides and phospholipids was completely inhibited by the lipase inhibitor Orlistat (40 μM). Interestingly, compared to Fusarium graminearum lipase (GZEL) and the Thermomyces lanuginosus lipase (Lipolase®), this novel fungal (phospho)lipase showed extreme tolerance to the presence of non-polar organic solvents, non-ionic and anionic surfactants, and oxidants, in addition to significant compatibility and stability with some available laundry detergents. The analysis of washing performance showed that it has the capability to efficiently eliminate oil-stains. Overall, FAL could be an ideal choice for application in detergents.

Molecular and functional characterization of protease from psychrotrophic Bacillus sp. HM49 in North-western Himalaya.

In this work, a psychrotrophic bacteria producing cold-active protease, was obtained from Dachigam National Park, an ecologically significant habitat in Western Himalayas owing to its varied endemic and endangered flora and fauna. This isolate was identified as Bacillus sp. HM49 via phenotypic, Gram staining, bio-chemical and 16S rRNA gene identification. Isolate HM49 when tested for proteolytic activity revealed prominent hydrolytic zone with the most production at 20 °C and pH, 8.0 post 72 h incubation. This enzyme was purified, enhancing its specific activity to 61.15 U/mg and its characterization studies revealed it to be a cold-alkaline protease being active in a wide pH (6.0-12) and temperature (5-40 °C) range. Amplification of CAASPR gene of HM49 was performed, followed by enzyme-substrate docking studies and MMGBSA providing details about its type, molecular weight validation as well as functional applications. The purified protease of HM49 was tested for laundry applications and the enzyme was found to be compatible with majority of the detergents tested. Its potential as an eco-friendly detergent additive was further validated by wash performance test as it effectively removed recalcitrant blood stains at a low temperature of 20 °C that could be beneficial for fine garments like silk which preferably need cold washing.

Isolation, screening and optimization of cellulase production by a novel bacterial isolate Enterococcus durans

Cellulose is an abundant plant biomass and a renewable source of energy in the ecosphere. The breakdown of cellulose occurs via the cellulase enzyme, which is commonly produced by microbes. This study aimed to optimize the fermentation parameters for enhanced cellulase production. Standardized parameters include isolation and screening of cellulase-producing bacteria (CPB), production of an enzyme, biochemical and molecular identification of bacterial isolate, optimization of cultural parameters, and application in wash performance. A total of 581 bacterial strains were isolated from soil samples, of which 16 isolates formed zones of hydrolysis on carboxymethylcellulose (CMC) agar media and were categorized as CPB. Based on maximum hydrolysis zone formation, three isolates, Krishi Vigyan Kendra-5 (KVK-5), Greenhouse-4 (GA-4), and Medicinal Garden-5 (MG-5) were chosen for bacterial cellulase production (BCP), with the isolate MG-5 proving to be the best cellulase producer (1.75 ± 0.01 U ml-1). Based on 16S rRNA gene sequencing the isolate MG-5 was identified as Enterococcus durans. The optimized parameters for the production of the cellulolytic enzyme were an incubation period of 48 h, CMC (carbon source), and yeast extract (nitrogen source) at a concentration of 1.5% w/v, pH 7, 45 °C, 1.5% v/v inoculum size and 100 rpm. Optimum conditions resulted in a 1.92-fold increase (3.36 U ml-1) in cellulase activity. Cellulase enzyme when used with detergent (Surf Excel), resulted in more efficient removal of chocolate stains on cotton fabric. This is the first report of Enterococcus durans producing cellulolytic enzymes. The analysis of cellulase in stain removal provides valuable evidence regarding the application of this enzyme in laundry cleaning.