Insight into the Interaction Between Carbopol® 940 and Ionic/Nonionic Surfactant

Mixtures of a cross‐linked polyacrylic acid (Carbopol^® 940) and two types of surfactants, namely anionic sodium dodecylsulfate (SDS) and nonionic Tween^® 80, were investigated by viscometry, conductometry, tensiometry, spectrophotometry, fluorimetry and scanning electron microscopy (SEM). The addition of nonionic surfactant decreased the reduced viscosity and the transmittance of the Carbopol^® polymer aqueous solutions. Furthermore, the interaction between Carbopol^® 940 and SDS was characterized by two significant concentration values: the critical aggregation concentration of SDS was particularly independent of Carbopol^® polymer concentration while the polymer saturation point of both surfactants increased with the increase in polymer content. The values of critical aggregation concentration and polymer saturation point obtained using various techniques confirmed the occurrence of Carbopol^® polymer–surfactant associations. The effect of different SDS and Tween^® 80 concentrations on the conformation of Carbopol^® 940 in aqueous solution could be explained through hydrophobic association between surfactant micelles and Carbopol^® polymer tails and through hydrogen bonding in the case of Tween^® 80. Additionally, the surfactant‐induced structural changes were confirmed in Carbopol^® 940–SDS and Carbopol^® 940–Tween^® 80 aqueous solutions by SEM measurements.     

An Analytically Defined Fire‐Suppressing Foam Formulation for Evaluation of Fluorosurfactant Replacement

A 4‐component, analytically defined, reference fluorosurfactant formulation (Ref‐aqueous film forming foam [AFFF]) composed of 0.3% fluorocarbon‐surfactant concentrate (Capstone 1157), 0.2% hydrocarbon‐surfactant concentrate (Glucopon 215 UP), and 0.5% diethylene glycol mono butyl ether by volume in distilled water was found to have rapid fire extinction comparable to a commercial AFFF in tests conducted on a bench scale and a large scale (28 ft², part of US Military Specification, MIL‐F‐24385F). The Ref‐AFFF was analytically characterized to provide the identity and quantity of the chemical structures of the surfactant molecules that were lacking for commercial AFFF formulations. To arrive at an acceptable Ref‐AFFF formulation, 3 candidate formulations containing different hydrocarbon surfactants in varying amounts were evaluated and ranked relative to a commercial AFFF using a bench‐scale fire‐extinction apparatus; varying the hydrocarbon surfactant was found to affect the fire‐extinction time. The ranking was confirmed by the large‐scale tests suggesting that the bench‐scale apparatus is a reasonable research tool for identifying surfactants likely to succeed in the large‐scale test. In the future, replacing the fluorocarbon surfactant with an alternative surfactant in the Ref‐AFFF enables a direct comparison of fire extinction and environmental impact to identify an acceptable fluorine‐free formulation.     

Production of thermostable alkaline lipase on vegetable oils from a thermophilic Bacillus sp. DH4, characterization and its potential applications as detergent additive

BACKGROUND: The alkaline lipase production on vegetable oils as sole carbon source, its characterization and effect of different commercial detergents and surfactants on enzymatic activity from thermophilic Bacillus sp. DH4 was investigated. RESULTS: The organism grew on mannose, but the amount of lipase secreted was significantly less than on vegetable oils. This study identified a simple substrate for lipase production and established the utility of groundnut oil for increasing the lipase yield. The enzyme was compatible with various ionic and non‐ionic surfactants as well as commercial detergents. Lipase activity was strongly inhibited by sodium dodecyl sulfate (SDS), but not by Triton X‐100 or Triton X‐114. The best assay conditions observed for this lipase was found to be pH 9.0 and 50 °C. The enzyme was stable at alkaline pH and considerable activity was observed at pH 10 and it retained 93% of the residual activity at 60 °C. The lipase showed a novel property of marked activation at alkaline pH. Wash performance analysis of commercial detergent for removal of fatty stains improved upon addition of lipase. CONCLUSION: The production on cheap vegetable oils, novel properties and resistance towards various surfactants and tolerance to commercial detergents make this lipase a potential additive for detergent formulations. Significance and impact of the study: Bacillus sp. produces alkaline and thermostable lipase on cheap vegetable oils and its compatibility can find use in the detergent industry. Copyright © 2008 Society of Chemical Industry     

Detergent‐Compatible Robust Alkaline Protease from Newly Isolated Halotolerant Salinicoccus sp. UN‐12

Currently, enzyme‐containing blended detergent preparations are favored in the detergent industry. The detergent compatibility of an enzyme depends on its robustness to withstand harsh operating conditions and maintain efficient functioning in the presence of various surfactants and detergents. Alkaline proteases from halotolerant microbes having the capability to work in demanding environments are desirable for their application in the detergent industry. The protease secreted by a halotolerant soil isolate Salinicoccus sp. UN‐12 was evaluated for its suitability in detergent formulations. The studied enzyme is an alkaline serine protease (63 kDa) with an optimum temperature of 55 °C and optimum pH of 8.5. The protease was purified 17‐fold with a 4% yield. The protease was active in NaCl (up to 4 mol) and showed enhanced activity in the presence of CaCl₂, KCl, and MnCl₂. In addition, the proteolytic activity was sustained in the presence of various organic solvents, cyclodextrin, disodium cocoamphodiacetate, ionic liquids, hydrotropes, and ultrasound. This report is the first to document the multifarious robustness and novel attributes of a protease secreted by the newly isolated Salinicoccus sp. UN‐12. The protease‐detergent formulation efficiently removes blood, egg, grass, and tomato sauce stains. This protease is now available for efficient and eco‐friendly applications in the detergent industry.     

Nonionic Mixed Surfactant Stabilized Water-in-Oil Microemulsions for Active Ingredient In Vitro Sustained Release

Olive oil is an excellent dispersing medium for water‐in‐oil microemulsions as it helps hydrate the skin and enhances the release of the active ingredients. In this study, mixed surfactants containing Span^® 80 with varied Tween^® series at 1:1 ratio were prepared with olive oil and water to produce water‐in‐oil microemulsions. The microemulsions were used to study the in vitro release of the active ingredients with different water solubilities. A microemulsion olive oil/water/mixed surfactant (56:4:40 by weight) was selected from the constructed phase diagram for further physical characterization. The analysis showed that the microemulsion composed of Span^® 80 and Tween^® 80 (ST80) was the most suitable surfactant combination. Equal amounts of ascorbic acid, caffeine and lidocaine were solubilized in ST80 microemulsions to study their release rate. Physical evaluation of ST80 microemulsions incorporating the active ingredients showed no apparent change compared to the ST80 microemulsion alone. The in vitro release study showed that the rate of active ingredients released from the microemulsion into the receptor chamber depends on their hydrophobicity, whereby lidocaine and caffeine were fivefold and twice as fast, respectively, with respect to ascorbic acid. ST80 microemulsions show constant rate of active ingredient release, demonstrating the sustained release properties of the system.     

Mixed Surfactant-Based Reverse Micellar Extraction Studies of Bovine Lactoperoxidase

The suitability of reverse micellar extraction for recovery of bovine lactoperoxidase (LP) from aqueous solution was evaluated using systems formed by ionic and nonionic surfactant mixtures. The influence of ionic surfactant concentration, organic solvent, and pH on the extraction of LP into the reverse micellar phase was studied. The Tween® series surfactants with Aerosol-OT (bis-(2-ethylhexyl) sulfosuccinate) showed better extraction of LP in the reverse micelles (RM) compared to the Triton® and Span® series of surfactants. Complete extraction of LP from an aqueous phase of initial concentration 25 mg L⁻¹ occurred with the RM formed by 90 mM Aerosol-OT/8 mM Tween® 80 in isooctane. The optimal pH, ionic strength, and positively charged ionic surfactant concentration for back extraction were also studied and a maximum of 95.5% back extraction efficiency and 66% LP activity recovery was obtained for a pH of 10.5,1 M KCl and 60 mM cetyltrimethylammonium bromide system.     

The Impact of Polyoxyethylene Sorbitan Surfactants in the Microstructure and Rheological Behaviour of Emulsions Made With Melted Fat From Cupuassu (<Emphasis Type="Italic">Theobroma grandiflorum</Emphasis>)

Cupuassu fat is a good candidate for partial substitution of cocoa butter in many products, including emulsions. However, for such use it is necessary to know the characteristics of the products prepared with cupuassu fat. Therefore, the main goal of this work is to characterize emulsions prepared with cupuassu fat using the surfactants Tween^® 60, Tween^® 80 and Tween^® 85 as emulsifiers. The emulsions were prepared at 43 °C with addition of 0.5 or 1.5 % (w/v) of surfactant and compared with an emulsion without surfactant. All emulsions were analysed by conductivity, stability, pH, optical microscopy, rheology and oxidative stability. It was verified that the emulsions prepared with Tween^® 60 and Tween^® 80 have higher stability, smaller droplet size and higher apparent viscosity. Also, these properties are positively influenced by the concentration of the surfactant. On the other hand, emulsions prepared with Tween 85 or without surfactant reached unsatisfactory results. The rheological behaviour of the emulsions was adequately described by both Herschel-Bulkley and Mizhari-Berki models revealing pseudoplastic character. These emulsions also present strong gel behaviour, with storage modulus higher than loss modulus. In conclusion, cupuassu fat can be used as oil phase for emulsions products and this characterization helps to understand their behaviour in order to increase their use in food industry.     

Detergent Compatible Extracellular Lipase from Streptomyces cellulosae AU‐10: A Green Alternative for the Detergent Industry

Enzymes can decrease the environmental and economic load of detergent products by reducing the amount of chemicals used in detergents and by allowing washing at ambient temperatures. In this study, Streptomyces cellulosae AU‐10 (GenBank accession number: MG780240) lipase was purified 7.08‐fold with 68% yield using an aqueous 2‐phase system. The Streptomyces sp. AU‐10 lipase showed maximal activity at pH 9.0 and 40 °C. Hundred percent activities were measured in the pH range from 9.0 to 11.0 for 1 h. The enzyme was also highly stable at 30–50 °C. The values of K_m and V_max were calculated as 0.34 mM and 0.83 mM min^?1, respectively. The lipase has high hydrolytic activity for olive oil and sunflower oil. The effect of ethylenediamine tetraacetic acid on the enzyme has shown that the lipase is a metalloenzyme. The activity increased in the presence of Fe²⁺, Cu²⁺, and various boron compounds. The enzyme has shown a good stability not only with surfactants but also with oxidizing agents. In addition, activities in the presence of Omo, Ariel, Tursil, Pril, and Fairy were measured as 108.8%, 115.6%, 98.35%, 140.4%, and 107.6%, respectively. Considering its remarkable ability, the S. cellulosae AU‐10 lipase can be considered as a potential additive in the detergent industry.     

Improving the properties of water-borne pressure sensitive adhesives by using non-migratory surfactants

The adhesive performance of high solids content water-borne acrylic pressure sensitive adhesives synthesized using polymerizable surfactants (Latemul^®PD-104 and Sipomer^®Pam-200) or a polymerizable stabilizer (Sipomer^®Cops-1) has been studied. The use of a high pH during the polymerization process has a deleterious effect on the final adhesive properties because gel polymer is not formed. Interestingly, at low pH it is found that the surfactant concentration used during the polymerization process has also an effect on the polymer microstructure; the higher the surfactant concentration, the higher the final gel content of the latex. When polymerizable surfactants or a stabilizer are used the peel strength of the final films is considerably improved due to the surfactant incorporation into the polymer backbone and hence reduced surfactant migration to the air-film interface. Work of adhesion and shear adhesion failure temperature (SAFT) are not noticeably affected by surfactant migration but their performance is affected by the surfactant employed.     

Enzyme-based detergent formulas for fatty soils and hard surfaces in a continuous-flow device

The present work analyzes the effect of incorporating a lipolytic enzyme (Lipolase^® 100L) into detergent formulas for washing fatty soils on hard surfaces. The experimental device, which is called a “bath-substrate-flow” device, uses a continuous flow on a substrate (glass spheres) soiled with triolein. Washing tests were done using only the enzyme and changing both its concentration and the temperature of the process. The results showed that, in the presence of lipase, soil removal was achieved through three consecutive mechanisms: (i) fundamental devoval of the soil by the bath flow through the experimental device; (ii) emulsion of the soil in the washing medium; and (iii) enzymatic hydrolysis of the dispersed soil. Different commercial surfactants were used, and detergency was evaluated in the absence and presence of lipase. The use of surfactant formulas with the lipolytic enzyme showed a positive effect of the enzyme on the detergency values registered with the fatty alcohol ethoxylate surfactants Findet^® 10/15 and Findet 1214N/23, and with the anionic surfactant linear alkylbenzene sulfonate. The commercial surfactants Glucopon^® 600, Glucopon 650, Findet 10/18, and Findet Q/21.5NF alone each presented high detergency values for fatty soils, and the effect of the incorporation of the lipase was not significant.     

Effect of Surfactants on Catalytic Activity of Diastase α-Amylase

The enzyme amylase is one of the hydrolyzing enzymes used in detergent formulation in order to remove soil based on polysaccharides. The effectiveness of the enzyme depends on its compatibility with other ingredients of the formulation. Among the studied additives, comprising anionic surfactants sodium dodecyl hydrogen sulfate (SDS) and dioctyl sodium sulfosuccinate, the cationic surfactant cetyl trimethyl ammonium bromide (CTAB), nonionic surfactants polyoxyethylene sorbitan monooleate and polyoxyethylene octyl phenyl ether, carboxy methyl cellulose and sodium sulfate, only the anionic surfactant SDS and cationic surfactant CTAB showed catalytic enhancement of α-amylase. The kinetic parameters, K _m and k _cat, showed an increase in catalytic activity in the micellar pseudophase. The decrease in optimum temperature from 55 to 30 °C and the shift in optimum pH from 5.5 to 7 on the addition of SDS and CTAB for the hydrolysis of starch are very favorable to enhance the washing characteristics.     

Cold Water Detergency of Triacylglycerol Semisolid Soils: The Effect of Salinity,Alcohol Type,and Surfactant Systems

Cold water detergency of triacylglycerol semisolid soils is much more challenging than liquid vegetable oils due to poorer interaction between surfactants and semisolid soil. This research seeks to improve the removal efficiency of semisolid soils below their melting points using surfactant-based formulations containing different alcohol additives. To this end, cold water detergency of solid coconut oil and solid palm kernel oil was investigated in various surfactant/alcohol systems, including single anionic extended surfactants, single nonionic alcohol ethoxylate surfactants, and a mixture of anionic surfactants. A series of alcohols (2-butanol, 1-hexanol, 1-heptanol, 1-octanol, 1-nonanol, and 1-decanol) were added to the surfactant formulations to investigate cold water detergency improvement. While cold water detergency using surfactants alone was poor, it was considerably improved when optimum salinity (S*) and 1-heptanol, 1-octanol, or 1-nonanol were introduced to the studied surfactant formulations. The maximum detergency of solid coconut oil exceeded 90% removal in the 0.1 w/v% C_14-15-8PO-SO₄Na/0.2 w/v% 1-octanol/4 w/v% NaCl system (a final optimized surfactant system) at a washing temperature of 10°C versus 22.9 ± 2.2% in the surfactant alone (not at optimum salinity and no additive). Further analysis showed that improved cold water detergency using surfactant/intermediate-chain alcohols/NaCl could be correlated with high wettability (low contact angle) as well as favorable surfactant system-soil interaction as observed by lower interfacial tension values. In contrast, the improved cold water detergency was observed to be independent of dispersion stability. This work thus demonstrates that surfactant system design, including additives, can improve cold water detergency of semisolid soils and should be further explored in future research.     

Characterization of Phosphate-Free Detergent Powders Incorporated with Palm C16 Methyl Ester Sulfonate (C16MES) and Linear Alkyl Benzene Sulfonic Acid (LABSA)

Laboratory and pilot scale investigations were carried out on phosphate-free detergent (PFD) formulations comprising binary anionic surfactants of C16 palm methyl ester sulfonates (C16MES) and linear alkyl benzene sulfonic acid (LABSA) with the aim of maximizing the incorporation of C16MES into low density detergent powders without compromising the detergency and other significant properties. Initial laboratory experiments revealed that the detergent powder resulting from C16MES/LABSA with a 50:50 ratio and pH 7–8 has acceptable detergency stability over 1 week of accelerated ageing test at 50 °C and 85 % relative humidity. Subsequent experiments were carried out in a 5-kg/h-capacity pilot spray dryer using PFD formulations of C16MES/LABSA over the whole range of weight ratios under the same pH of 7–8. The concentration of the detergent slurry and cleaning performance (detergency, foaming ability and wetting power) of the resulting spray dried detergent powder (SDDP) were evaluated. C16MES/LABSA in a 40:60 ratio was selected as the ideal formulation based on its optimum detergent slurry concentration and comparable cleaning performance against the control formulation. Further environmental tests have confirmed that SDDP obtained from the ideal formulation is readily biodegradable (60 % in 13 days) and exhibits low eco-toxicity properties (LC₅₀ of 11.3 mg/L).     

Production,Biochemical Characterization and Detergents Application of Keratinase from the Marine Actinobacterium Actinoalloteichus sp. MA-32

The present study is the first report on poultry feathers as a novel, inexpensive substrate for the production of a thermo‐ and detergent stable keratinase from a marine actinobacterium belonging to the genus Actinoalloteichus. Medium composition and culture conditions for the keratinase production by Actinoalloteichus sp. MA‐32 were optimized using two statistical methods: Plackett–Burman design was applied to find the key ingredients and conditions for the best yield of enzyme production and central composite design used to optimize the concentration of the five significant variables: whole chicken feather, soy flour, MgSO₄·7H₂O, KH₂PO₄ and NaCl. The medium optimization resulted in a 19.30‐fold increase with a 31.99 % yield with a specific activity of 3842.57 U mg^?1 and the molecular weight was estimated as 66 kDa. The enzyme was optimally active at pH 8–10 and temperature 50–60 °C and it was most stable up to pH 12 and 10–14 % of NaCl concentration. The enzyme activity was reduced when treated with Hg²⁺, Pb²⁺, Tween‐80, 1,10‐phenanthroline and EDTA and stimulated by Fe²⁺, Mg²⁺, Cu²⁺, Ca²⁺, Ni²⁺, Mn²⁺, SDS, ethoxylated (9.5EO) octylphenol, DMSO, sodium sulfite and β‐mercaptoethanol. The keratinase exhibited a significant stability and compatibility with most of the tested commercial laundry detergents, demonstrating its feasibility for inclusion in laundry detergent formulation. These results suggest that this extracellular keratinase may be a useful alternative and eco‐friendly route for handling the abundant amount of waste feathers or for applications in detergent formulation and other industrial processes.     

Use of certain alcohol ethoxylates to maintain protease stability in the presence of anionic surfactants

Anionic surfactants, including linear alkylbenzene sulfonate (LAS), are known to decrease the stability of detergent proteases, possibly by hastening autoproteolytic processes. Thus, protease shelf life in enzyme-containing, heavy-duty liquid laundry detergents (HDL) is typically maintained by adding stabilizers, by limiting the level of interfering anionics, or by utilizing more compatible anionics, such as alcohol ethoxysulfates (AES). This study examines the stability of Savinase^® detergent protease in HDL formulations based on LAS and containing different alcohol ethoxylates (AE) for protection against protease inactivation. Dose response curves demonstrated that all commonly used anionic surfactants except AES promote loss of protease activity. In HDL formulations with equal percentage compositions of LAS and AE, the structure of the selected AE was found to have a profound influence on protease stability. Inclusion of AE with chain length ≥C₁₄ and ethoxylate levels >70% resulted in greater protease stability. HDL containing LAS and these protective AE could be formulated to achieve protease stability matching those of simulated commercial products. Unlike polyhydric stabilizers, the AE by themselves confer no additional stability to the protease. It is more likely that the stabilizing effect of the “protective” AE is due to decreased availability of LAS to the protease.     

Hard-Surface Cleaning Using Lipases: Enzyme–Surfactant Interactions and Washing Tests

A commercial lipase (E.C. 3.1.1.3) from Thermomyces lanuginosus was studied in order to assess its interaction with commercial nonionic (Findet^® 1214N/16, Findet 1214N/23 and Glucopon^® 650) and anionic (linear alkylbenzene sulphonate; LAS) surfactants, as well as the cleaning action exerted by the enzyme on hard surfaces. Nonionic surfactants seem to prevent or delay enzyme penetration at the interface, thereby decreasing lipase activity. Notably, no inhibitory effect of the anionic surfactant LAS on lipase action was found, higher conversions being achieved after 20 min of enzymatic hydrolysis in the presence of this surfactant than in its absence. A device for testing detersive performance, the so-called bath–substrate–flow, was used in washing experiments with the lipase at different temperatures with or without surfactant. Employing two different oily stains (tributyrin and triolein), it was found that the lipase by itself increases detergency significantly, preventing the subsequent redeposition of the removed dirt. Expressions relating detersive efficiency to lipase concentration and temperature were obtained using "Statistical Design of Experiments" methodology.     

Investigation of the impact of latex components on the survival ofPseudomonas Aeruginosa

Control of biological spoilage is critical to the success of any coatings formulation. However, problems with bacterial resistance and biocide toxicity require changes in waterborne resin preparation and the resulting formulated product. Despite the importance of controlling bacteria-induced spoilage, very little research exists in the field. Critical aspects of biocide/bacteria/coatings component interactions must be understood in order to improve the design of future biocides specific for coatings formulations. This research examines the impact of several common latex components and model biocide interactions on the survival ofPseudomonas aeruginosa. Systems were characterized using both traditional microbiological techniques and a novel high-throughput fluorescence technique.P. aeruginosa is recognized as the most problematic bacterium throughout the coatings industry because of its tendency to quickly develop resistance to both antibiotics and biocides. Designed experiments comparing formulations of 10% surfactant (by weight) reveal that formulation combinations rich in ionic surfactants promote bacterial growth compared to formulations with higher concentrations of nonionic surfactants. Studies also reveal that the ionic nature of the surfactant components has a strong impact on both the rate ofP. aeruginosa survival as well as biocide efficiency, with gentamicin sulfate activity being strongly inhibited in formulations containing high concentrations of sulfated surfactant. Presented, in part at the 31st Annual International Waterborne, High-Solids and Powder Coatings Symposium, New Orleans, LA, 2004. School of Polymers and High Performance Materials. Dept. of Biological Sciences.     

The Use of Boron Compounds for Stabilization of Lipase from Pseudomonas aeruginosa ES3 for the Detergent Industry

This study aimed to characterize a lipase that is highly active and stable under typical washing conditions for use as a detergent ingredient by investigating the effects of various boron compounds on lipase stabilization under different conditions. In addition, the antimicrobial activity of the boron compounds used in enzyme stabilization was examined in order to obtain an effective antimicrobial detergent. A lipase‐producing bacterium was isolated from kitchen wastewater samples using Rhodamine‐B Agar medium and identified as Pseudomonas aeruginosa based on 16S rDNA sequence analysis. The ES3 lipase obtained from P. aeruginosa was purified, and the purified enzyme was found to have a molecular mass of 40 kDa. The enzyme showed optimal activity at pH 9.0–10.0 and 40 °C and remained stable in the presence of various metal ions, surfactants and oxidizing agents. Moreover, the pH stability and thermostability of the enzyme was improved by the addition of boron compounds, which, when used as stabilizers in the incubation media, also increased the stability of the enzyme towards commercial detergents. Furthermore, the enzyme displayed properties comparable with the commercial product Lipolase^®, which has shown excellent stability towards various commercial detergents. Finally, boron compounds used to stabilize the lipase were found to possess antimicrobial properties, suggesting that detergents incorporating these compounds will also exhibit antimicrobial activity when washing clothes and dishes.     

Calcium Chelating Sugar-Based Surfactants for Hard-Water Detergency

Hard water can decrease the detergency efficiency of surfactants due to a significant concentration of divalent cations as Ca²⁺ or Mg²⁺. The formulation of a cleaning detergent must be modified and it is usual to add more surfactants or a huge quantity of sequestrating agents. This supplementary addition can have deleterious effects on the environment and increases the price of the formulation. A surfactant, presenting both detergency capacities in the presence of Ca²⁺ and Ca²⁺ chelating properties, would be of great interest. In this paper, we report on Ca²⁺ extraction with sugar-based chelating surfactants using an experimental device, namely a flotation column, as both chelating properties and foaming properties in the presence of Ca²⁺ are important in the flotation process as well as in detergency. Among all the sugar-based surfactants tested, a few of them were able to extract calcium and thus demonstrated the expected characteristics.     

Burkholderia multivorans SB6 Lipase as a Detergent Ingredient: Characterization and Stabilization

In this study, 265 bacterial isolates were collected from kitchen wastewater samples using Rhodamine B agar medium. Of these, 115 isolates were found to respond positively to the addition of commercial detergents. Using 16S rRNA sequence analysis, the isolate demonstrating the high stability towards commercial detergents was identified as Burkholderia multivorans. An SB6 lipase with a molecular mass of 70 kDa was purified from B. multivorans. The purified enzyme showed optimal activity at pH 9.0 and 40 °C and remained stable in the presence of various metal ions, surfactants, and oxidizing agents. The addition of boron compounds improved the pH stability and thermostability of the enzyme, which displayed stability against some commercial detergents; moreover, this stability increased when boron compounds were added to the incubation medium as stabilizers. These properties make SB6 lipase an ideal choice as an additive in detergent formulations.