Commercial Detergents Research Articles

RSM-Based Optimization Approach in Production of Anionic Methyl Ester Sulfonate for Commercial Detergent Application

RSM-Based Optimization Approach in Production of Anionic Methyl Ester Sulfonate for Commercial Detergent Application

Detergents containing cationic hydroxyethyl cellulose: Benefits on dark garments leveraging a consumer relevant wash method

AbstractThe industrial standard methods to evaluate color care of detergents leverage technical fabrics and use known dye standards from A.I.S.E. (International Association for Soaps, Detergents and Maintenance Products). This has some limitations: (1) it is not always following the latest fashion trends; (2) overall color fading of a garment is due to both dye bleeding out of the fabric as well as friction during the wash leading to fabric texture changes. The latter depends on parameters such as fabric type and surface area that could be better assessed on real garments. To overcome the above limitations, we have designed a new protocol considering the incidence of garment types, fiber and dye chemistry. Leveraging this protocol, we assessed the effect of the presence of a cationic hydroxyethyl cellulose in a commercial detergent formulation on dark fabrics/garments. Our results indicate that the commercial detergent formulation with cationic hydroxyethyl cellulose delivers dark/black color benefit.

Production and characterization of activated carbon from pineapple stubble for removal of methylene blue and surfactants.

The objective of this work was to produce activated carbon from the agricultural waste known as pineapple stubble, and to test its effectiveness in the removal of methylene blue and surfactants. Activated carbon was prepared using ZnCl2 and H3PO4 as activating agents and impregnation ratios of 2: 1 and 4:1 between the agent (mL) and the precursor (g) were evaluated. It was also investigated the need or not of a drying stage prior to carbonization. The produced activated carbon was characterized through FT-IR spectroscopy, X-ray fluorescence, N2 physisorption analysis, elemental analysis and electron microscopy. Methylene blue adsorption tests were performed to determine the adsorption effectiveness of the different activated carbons produced. For such evaluation, a 23 factorial design was used, and statistical analysis determined that the activated carbon with the highest adsorption of methylene is produced under the following conditions: ZnCl2 as activating agent, an impregnation ratio of 4:1 and with no drying step prior to carbonization. This produced activated carbon is also effective in the adsorption of the surfactant sodium dodecyl sulfate and for the surfactants present in the gray water obtained after washing clothes with commercial detergent. In these cases, removal efficiencies above 98 % were achieved. With respect to the characteristics of this activated carbon, it was observed a surface area of ​​685.5 m2/g, a total pore volume of 0.53 cm3/g, and an average pore diameter of 3.1 nm. Results achieved in the present study demonstrate that is possible to produce effective activated carbon for the removal of methylene blue and surfactants from an agricultural waste such as pineapple stubble.

An uncharacterized protein from the metagenome with no obvious homology to known lipases shows excellent alkaline lipase properties and potential applications in the detergent industry.

A novel lipase, Lip486, which has no obvious homology with known lipases, was discovered using functional metagenomics technology. Phylogenetic tree analysis suggested that the enzyme belongs to a new subfamily called lipolytic enzyme family II. To explore the enzymatic properties, lip486 was expressed heterologously and efficiently in Escherichia coli. The recombinant enzyme displayed the highest activity on the substrate p-nitrophenyl caprate with a carbon chain length of 10, and its optimum temperature and pH were 53°C and 8.0, respectively. The recombinant Lip486 showed good activity and stability in strong alkaline and medium-low-temperature environments. The results of compatibility and soaking tests showed that the enzyme had good compatibility with 4 kinds of commercial detergents, and an appropriate soaking time could further improve the enzyme activity. Oil stain removal test results for a cotton cloth indicated that the washing performance of commercial laundry detergent supplemented with Lip486 was further improved. In addition, as one of the smallest lipases found to date, Lip486 also has the advantages of high yield, good stability and easy molecular modification. These characteristics reflect the good application prospects for Lip486 in the detergent and other industries in the future.

Multipotential Alkaline Protease From a Novel Pyxidicoccus sp. 252: Ecofriendly Replacement to Various Chemical Processes.

A newly isolated alkaline protease-producing myxobacterium was isolated from soil. The strain was identified as Pyxidicoccus sp. S252 on the basis of 16S rRNA sequence analysis. The extracellular alkaline proteases produced by isolate S252 (PyCP) was optimally active in the pH range of 11.0–12.0 and temperature range of 40–50°C The zymogram of PyCP showed six caseinolytic protease bands. The proteases were stable in the pH range of 8.0–10.0 and temperature range of 40–50°C. The activity of PyCP was enhanced in the presence of Na+, Mg2+, Cu2+, Tween-20, and hydrogen peroxide (H2O2) (hydrogen peroxide), whereas in Triton X-100, glycerol, ethylenediaminetetraacetic acid (EDTA), and Co2+, it was stable. PyCP showed a potential in various applications. The addition of PyCP in the commercial detergent enhanced the wash performance of the detergent by efficiently removing the stains of tomato ketchup and coffee. PyCP efficiently hydrolyzed the gelatin layer on X-ray film to release the embedded silver. PyCP also showed potent dehairing of goat skin and also efficiently deproteinized sea shell waste indicating its application in chitin extraction. Thus, the results of the present study indicate that Pyxidicoccus sp. S252 proteases have the potential to be used as an ecofriendly replacement of chemicals in several industrial processes.

Artificial Neural Networks and Response Surface Methodology Approach for Optimization of an Eco-Friendly and Detergent-Stable Lipase Production from Actinomadura Keratinilytica Strain Cpt29

This work mainly focused on the production of an efficient, economical, and eco-friendly lipase (AKL29) from Actinomadura keratinilytica strain Cpt29 isolated from poultry compost in north east of Algeria, for use in detergent industries. AKL29 shows a significant lipase activity (45 U/mL) towards hydrolyzed triacylglycerols, indicating that it is a true lipase. For maximum lipase production the modeling and optimization of potential culture parameters such as incubation temperature, cultivation time, and Tween 80 (v/v) were built using RSM and ANN approaches. The results show that both the two models provided good quality predictions, yet the ANN showed a clear superiority over RSM for both data fitting and estimation capabilities. A 4.1-fold increase in lipase production was recorded under the following optimal condition: incubation temperature (37.9 °C), cultivation time (111 h), and Tween 80 (3.27%, v/v). Furthermore, the partially purified lipase showed good stability, high compatibility, and significant wash performance with various commercial laundry detergents, making this novel lipase a promising potential candidate for detergent industries.

Highly Efficient Computationally Derived Novel Metagenome α-Amylase With Robust Stability Under Extreme Denaturing Conditions.

α-Amylases are among the very critical enzymes used for different industrial purposes. Most α-amylases cannot accomplish the requirement of industrial conditions and easily lose their activity in harsh environments. In this study, a novel α-amylase named PersiAmy1 has been identified through the multistage in silico screening pipeline from the rumen metagenomic data. The long-term storage of PersiAmy1 in low and high temperatures demonstrated 82.13 and 71.01% activities after 36 days of incubation at 4 and 50°C, respectively. The stable α-amylase retained 61.09% of its activity after 180 min of incubation at 90°C and was highly stable in a broad pH range, showing 60.48 and 86.05% activities at pH 4.0 and pH 9.0 after 180 min of incubation, respectively. Also, the enzyme could resist the high-salinity condition and demonstrated 88.81% activity in the presence of 5 M NaCl. PersiAmy1 showed more than 74% activity in the presence of various metal ions. The addition of the detergents, surfactants, and organic solvents did not affect the α-amylase activity considerably. Substrate spectrum analysis showed that PersiAmy1 could act on a wide array of substrates. PersiAmy1 showed high stability in inhibitors and superb activity in downstream conditions, thus useful in detergent and baking industries. Investigating the applicability in detergent formulation, PersiAmy1 showed more than 69% activity after incubation with commercial detergents at different temperatures (30–50°C) and retained more than 56% activity after incubation with commercial detergents for 3 h at 10°C. Furthermore, the results of the wash performance analysis exhibited a good stain removal at 10°C. The power of PersiAmy1 in the bread industry revealed soft, chewable crumbs with improved volume and porosity compared with control. This study highlights the intense power of robust novel PersiAmy1 as a functional bio-additive in many industrial applications.

Statistical optimization of thermostable alkaline protease from Bacillus cereus KM 05 using response surface methodology

Proteases have gained great attention due to their enormous applications in food, tannery, detergent, photography and many other industries. Proteases rank third position in the production of enzymes. This paper targets to isolate a bacterium with high alkaline protease activity and optimization of its production conditions using Response Surface Methodology (RSM). A bacterium isolated from soil contaminated with detergent exhibited clearance zone on skim milk agar medium with a protease activity of 22 U/ml. The bacterial strain was identified as Bacillus cereus KM05 and optimization of its production conditions were performed using statistical methods. Further optimization with Box Behnken design resulted in an increase in protease activity by 1.5-fold (28.6 U/ml). The protease enzyme was thermotolerant up to 70°C with stability towards alkaline pH (pH 9). The enzyme was not affected by most of the metal ions and solvents. Moreover, the protease was also compatible with six commercial detergents tested. Densitometric analysis of the destained fabric materials following the detergent-enzyme treatment, revealed a stain removal efficiency of 97%. The alkaline protease enzyme obtained was stable at different conditions with stain removal efficacy. Hence, the present alkaline protease could be used for detergent formulations.

The use of different detergents in skeletal preparations

Skeletal preparation has become an integral component within the field of forensic anthropology. The aim of this study was to determine which commercial detergent was most effective and efficient for use in skeletal preparation. The hind limbs of 24 pigs (Sus scrofa) and five detergents with bleaching agents and enzymes (Surf and Ariel), only enzymes (OMO Auto and Sunlight powder) or only bleaching agents (Sunlight dishwashing liquid) were used. Specimens were skinned and immersed into a pre-heated 6 L detergent solution or tap water and macerated at either 45 °C, 50 °C, 55 °C and 60 °C. When maceration was deemed complete any remaining soft tissue was manually removed under running tap water and the remains left to dry. A scoring system was utilized to assess the effectiveness and efficiency of each detergent. OMO Auto specimens only required a single day to complete macerate regardless of the temperature and these specimens constantly scored better than the other detergents used, thus making it the most effective and efficient detergent tested.

Detergent stable thiol-dependant alkaline protease produced from the endophytic fungus Aspergillus ochraceus BT21: Purification and kinetics

Proteases have different industrial applications thus to increase their yield and reduce the production cost; a low cost fermentation medium was designed for large scale production. From seven tested agro-wastes, wheat bran (1.0 g%) was found to increase the overall yield of alkaline protease from Aspergillus ochraceus BT21 more than 2 fold (7359.8 U/mg) compared to the control (optimized fermentation conditions obtained from our previous study). The enzyme was purified to homogeneity using ammonium sulphate precipitation, Sephacryl S-200, followed by DEAE-Sepharose and CM-Sepharose chromatography. The efficiency of the purification steps was confirmed by SDS–PAGE where, the molecular mass of the enzyme was 59.0 KDa. The purification fold was 15.13 with specific activity reached 111379.5 U/mg and 59.7% recovery. The enzyme was alkaline thermo-tolerant with optimum values of temperature and pH at 50 °C and 8.0, respectively. The purified enzyme was stable in a wide range of temperature (20–60 °C) and pH (5.0–11.0), and its maximum activity was observed with casein substrate. The inhibition studies showed that it is a thiol-dependant serine protease. The enzyme exhibited good stability with the commercial detergents. The specific properties of the purified enzyme suggested it is suitable for future industrial applications especially in detergent formulations.

Effective bioconversion of feather-waste Keratin by Thermo-Surfactant Stable Alkaline Keratinase produced from Aspergillus sp. DHE7 with promising biotechnological application in detergent formulations

Keratin-rich wastes are troublesome pollutants that their accumulation could lead to environmental problems. Microbial degradation of keratin wastes has emerged as an alternative bio-catalyst to steam-pressure cooking and alkali hydrolysis for the recycling of such residues to value-added products. The current work investigates the purification and biochemical characterisation of an extracellular keratinase from new Aspergillus sp. DHE7 using turkey feathers as substrate. The enzyme was purified 31-fold with a final yield of 37.5%. Purified keratinase is monomeric and its molecular mass was estimated to be 33 kDa as demonstrated on SDS-PAGE. The enzyme was active in wide range of pH (7.0–11) and temperature (37–70 °C) profiles with maximum activity at pH 8.5 and 60 °C. The activity was strongly suppressed by phenylmethylsulfonyl fluoride (93.4% inhibition) and moderately inhibited by EDTA (41.2% inhibition), suggesting that the current keratinase belongs to serine-metalloprotease. Bivalent cations, such as Ca2+, Zn2+, and Mn2+, enhanced enzyme activity by 165.7%, 176.3%, and 194.8%, respectively. The purified keratinase exhibited a wide proteolytic activity towards soluble and insoluble protein substrates displaying its greater activity toward casein, keratin, bovine serum albumin, and gelatin, followed by feathers, goat hair, and wool, and was substantially stable and compliant with surfactants and commercial laundry detergents. The Km, Vmax, Kcat and Kcat/Km values on keratin were 2.2 mg/mL, 2702.7 U/mL, 136.5 s−1 and 62.04 (s−1/mg mL−1), respectively. According to these characteristics, Aspergillus sp. DHE7 keratinase is suggested as a potential candidate for use in detergent formulations (as an additive) and in various biotechnological applications.

Statistical optimization of a novel extracellular alkaline and thermostable amylase production from thermophilic Actinomadura keratinilytica sp. Cpt29 and its potential application in detergent industry

Amylolytic enzymes are biocatalysts, which are widely used in several industrial sectors. The present study was carried out to investigate amylase production by a thermophilic actinobacteria strain Actinomadura keratinilytica Cpt29. Initially, optimization of nutritional and environmental factors was performed using the One Variable at Time (OVAT) approach and Plackett–Burman design. Further, the optimum level of each factor was determined using Box–Behnken design (BBD). The different investigations employed showed that corn starch and tryptone were found to be the best carbon and nitrogen sources, respectively. Corn starch, tryptone, and pH seem to be the most influential variables for amylase production. Enhancement of 1.5-fold in the catalytic activity was reached after optimization. The obtained enzyme was characterized. Optimal enzyme activity was recorded with an alkaline pH of 8.0 at 70 °C and significantly enhanced by Ca 2+ and Mg 2+ . Good stability was retained over a broad range of pH and temperature. Also, the obtained amylase showed strong tolerance to the commercial detergents tested and excellent cleaning efficiency, which makes this enzyme an interesting new additive for detergent formulations. • Actinomadura keratinilytica Cpt29 thermophilic actinomycete used for amylase production. • Corn starch and tryptone are the best carbon and nitrogen sources according to the One-factor-at-a-time optimization. • Enhancements of 1.5 fold in amylase production with the Response Surface methodology optimization. • The amylase from Actinomadura keratinilytica Cpt29 exhibited promising properties for biotechnological applications.

Solvent-Based Elimination of Organic Matter from Marine-Collected Plastics

The physical-chemical characterization of plastic litter from the marine environment requires the prior removal of the biofouling attached to their surface without causing any degradation in the polymer. The absence of a standardized protocol for digesting biofouling and organic matter of both macro and microplastic samples extracted from seawater has been the main motivation for this research work, which aims to evaluate the effectiveness of different solvents (hydrogen peroxide, ethanol, a commercial enzymatic detergent, and potassium hydroxide) for the digestion of organic matter and biofouling in different samples recovered from the Spanish Atlantic and Mediterranean coast. Moreover, the potential effect of those solvents on the physical-chemical structure of polymers, four virgin plastic reference materials (low-density polyethylene, polyamide, poly(ethylene terephthalate) and polystyrene) without any type of prior degradation has been characterized in terms of Fourier transform infrared spectroscopy (FTIR) and optical microscopy. Results indicate that the hydrogen peroxide at 15% concentration applied for one week at 40 °C is the most effective solvent for organic matter and biofouling removal, without causing any apparent damage on the structure of plastic samples analyzed.

Green detergent made of halloysite nanotubes

The detergent has wide range of applications and plays a critical role in daily life. However, the existing commercial detergents present the drawbacks of irreversible environmental pollution due to their discharge with wastewater. Herein, halloysite clay nanotube (HNT) with unique hollow structure was explored as a green, non-toxic, multifunctional, and cheap detergents. HNT has large aspect ratio, small size, and high adsorption ability, which provides the possibility for removing various stains from different substrates. The increased contact angle and decreased surface tension of HNT dispersion are achieved by increasing the HNT concentration, and HNT tends to stabilize oil-in-water (O/W) Pickering emulsion. The cleaning capacity of HNT on cotton fabric for dyes is almost twice that of laundry powder, indicating that highly efficient cleaning capability of HNT. HNT detergent is also effective to remove ink, tea, and chili oil from textiles with clean efficacy higher than 88%. As kitchen detergent, HNT can effectively eliminates chili oil from ceramic, stainless steel, glass, and plastic plate. Seed germination and crop growth experiment demonstrate that HNT detergent shows no toxicity towards plants and no contamination towards soil. Furthermore, the residue on the cloth of HNT detergent is negligible. Overall, HNT has great potential as an alternative detergent in the future because of its excellent cleaning efficacy and ecological friendliness.

Lipozyme 435-Mediated Synthesis of Xylose Oleate in Methyl Ethyl Ketone.

In this paper, we have performed the Lipozyme 435-catalyzed synthesis of xylose oleate in methyl ethyl ketone (MEK) from xylose and oleic acid. The effects of substrates’ molar ratios, reaction temperature, reaction time on esterification rates, and Lipozyme 435 reuse were studied. Results showed that an excess of oleic acid (xylose: oleic acid molar ratio of 1:5) significantly favored the reaction, yielding 98% of xylose conversion and 31% oleic acid conversion after 24 h-reaction (mainly to xylose mono- and dioleate, as confirmed by mass spectrometry). The highest Lipozyme 435 activities occurred between 55 and 70 °C. The predicted Ping Pong Bi Bi kinetic model fitted very well to the experimental data and there was no evidence of inhibitions in the range assessed. The reaction product was purified and presented an emulsion capacity close to that of a commercial sugar ester detergent. Finally, the repeated use of Lipozyme 435 showed a reduction in the reaction yields (by 48 and 19% in the xylose and oleic acid conversions, respectively), after ten 12 h-cycles.

Catalytic Performance of a Recombinant Organophosphate-Hydrolyzing Phosphotriesterase from Brevundimonas diminuta in the Presence of Surfactants

Phosphotriestease (PTE), also known as parathion hydrolase, has the ability to hydrolyze the triester linkage of organophosphate (OP) pesticides and chemical warfare nerve agents, making it highly suitable for environment remediation. Here, we studied the effects of various surfactants and commercial detergents on the esterase activity of a recombinant PTE (His6-tagged BdPTE) from Brevundimonas diminuta. Enzymatic assays indicated that His6-tagged BdPTE was severely inactivated by SDS even at lower concentrations and, conversely, the other three surfactants (Triton X-100, Tween 20, and Tween 80) had a stimulatory effect on the activity, especially at a pre-incubating temperature of 40 °C. The enzyme exhibited a good compatibility with several commercial detergents, such as Dr. Formula® and Sugar Bubble®. The evolution results of pyrene fluorescence spectroscopy showed that the enzyme molecules participated in the formation of SDS micelles but did not alter the property of SDS micelles above the critical micelle concentration (CMC). Structural analyses revealed a significant change in the enzyme’s secondary structure in the presence of SDS. Through the use of the intentionally fenthion-contaminated Chinese cabbage leaves as the model experiment, enzyme–Joy® washer solution could remove the pesticide from the contaminated sample more efficiently than detergent alone. Overall, our data promote a better understanding of the links between the esterase activity of His6-tagged BdPTE and surfactants, and they offer valuable information about its potential applications in liquid detergent formulations.

Optimization of protease production from Bacillus halodurans under solid state fermentation using agrowastes.

Marine microbes are potential source for novel metabolites. They are efficient in producing these metabolites utilizing agrowastes. Protease is one of the enzymes which find wide industrial applications. In the present study, protease producing bacteria was isolated from marine sediments and the organism was identified as Bacillus halodurans. The organism was subjected to protease production under solid state fermentation (SSF) using different agrowastes as substrates. Among the substrates used, wheat bran yielded maximum quantity of protease. The fermentation process was carried out under different cultural conditions to optimize the parameters influencing the enzyme production. The results of the stain removal studies by the enzyme revealed the increased efficiency of the microbial enzyme than the commercial detergent.

Optimization, purification, and biochemical characterization of thermoalkaliphilic lipase from a novel Geobacillus stearothermophilus FMR12 for detergent formulations

This study was aimed to produce a high compatible thermoalkaliphilic lipase (TA) with detergents from new thermophilic bacterial strains utilizing fish wastes for industrial application. Among bacterial isolates, a new Geobacillus stearothermophilus FMR12 efficiently utilized fish wastes at a concentration of 20% (w/v), exhibiting highly lipolytic activity at extreme thermal and alkaline pH conditions. Optimized fermentation parameters of TA lipase production were ascertained, promoting the productivity of the TA lipase from 424 to 1038 U/ml. Purification results of TA lipase exposed prominent specific activity of 4788 U/mg, purification fold of 12.44, and 7.8% yield. The purified TA lipase demonstrated outstanding activity and stability in a temperature range of 40–95 °C and pH (4–11), revealing optimal activity at 70 °C and pH 9. The molecular weight of the enzyme was estimated to be 63 kDa. Compared to control, the TA lipase activity was promoted in the presence of calcium chloride. Likewise, Triton X-100 enhanced the activity of the TA lipase, recording 128% of the control enzyme. Interestingly, the TA lipase conserved higher than 90% of its activity after blending with commercial detergents, emphasizing its competence for detergent formulations.

Development of xylanase as detergent additive to improve laundry application

The development of kitchen waste from UNISEL’s cafeteria as a substrate in the production of xylanase is an alternative way of converting waste to wealth. The production of xylanase as a detergent or detergent additive capable of removing plant stains compared to limited detergent applications that are unable to remove plant stains. Aspergillus niger was used in this study to degrade hemicellulose in kitchen waste and to secrete xylanase by solid state fermentation (SSF). Optimization of SSF parameters including substrate moisture content, inoculum size and incubation temperature were determined to optimize xylanase production. The finding of maximum activity of xylanase was identified at 80% of the moisture content, 8.0 mL of inoculum size and 30°C of the incubation temperature. The efficacy of xylanase (from optimized SSF parameters) as a plant stain remover is significantly effective compared to the commercial detergent used in this research. However, the mixture of detergent and xylanase can cause the chemical content of the detergent to interfere with the action of the enzyme and its efficacy in the removal of plant stains is less effective. It is also easier to use xylanase with water due to it is capable of producing excellent performance. This study demonstrated the high efficiency of the washing process using xylanase from kitchen waste and can be suggested for the laundry industry.

Production of Cross-Linked Lipase Crystals at a Preparative Scale.

The autoimmobilization of enzymes via cross-linked enzyme crystals (CLECs) has regained interest in recent years, boosted by the extensive knowledge gained in protein crystallization, the decrease of cost and laboriousness of the process, and the development of potential applications. In this work, we present the crystallization and preparative-scale production of reinforced cross-linked lipase crystals (RCLLCs) using a commercial detergent additive as a raw material. Bulk crystallization was carried out in 500 mL of agarose media using the batch technique. Agarose facilitates the homogeneous production of crystals, their cross-linking treatment, and their extraction. RCLLCs were active in an aqueous solution and in hexane, as shown by the hydrolysis of p-nitrophenol butyrate and α-methylbenzyl acetate, respectively. RCLLCs presented both high thermal and robust operational stability, allowing the preparation of a packed-bed chromatographic column to work in a continuous flow. Finally, we determined the three-dimensional (3D) models of this commercial lipase crystallized with and without phosphate at 2.0 and 1.7 Å resolutions, respectively.