Detergent Formulations Research Articles

The investigation of oxidative bleaching performance of peripherally Schiff base substituted tri-nuclear cobalt-phthalocyanine complexes

This study covers the functional complexes of tetrakis [4-(salicyhydrazone)phenoxy)] phthalocyaninato cobalt (II) (5) which was the macro molecular Schiff base ligand and synthesized through a multistep reaction sequence starting first with the cyclotetramerization of 4-[4-(1,3-Dioxolan-2-yl)phenoxy]-phthalonitrile (2). Then, the de-protection of tetra acetal groups of Tetrakis[4-(1,3-dioxolan-2-yl)phenoxy)]phthalocyaninato cobalt (II) (3) to the aldehyde functionality in acetic acid/FeCl3 system to yield the Tetrakis(4-formylphenoxy)phthalocyaninato cobalt(II) (4) and then its condensation with salicylhydrazide gave to 5. Finally, CoPc-bis(salicyhydrazone)phenoxy)manganese (III) (6), CoPc-bis(salicyhydrazone) phenoxy)cobalt(III) (7) and CoPc-bis (salicyhydrazone)phenoxy) nickel(II) (8) were synthesized using with the related MnCl2·4H2O, CoCl2·6H2O, Ni(CH3COO)2 salt in basic conditions in DMF. FT-IR, UV–Vis, MS spectra and elemental analysis were applied to characterize to prepared compounds.The bleaching performances of the prepared phthalocyanine compounds (3–8) were examined by the degradation of Morin as the hydrophilic dye which characterized the wine stains on the fabrics. Progress of the degradations in the catalysts (3–8)/H2O2 combination in basic aqueous solution conditions was investigated by using online spectrophotometric method (OSM). It was found that the prepared catalysts showed better bleaching performance at 25°C than to that of tetraacetylethylenediamine (TAED) bleach activator commercially used in powder detergent formulations.

ANCUT2, a Thermo-alkaline Cutinase from Aspergillus nidulans and Its Potential Applications

Biochemical characterization of purified ANCUT2 cutinase from Aspergillus nidulans is described. The identified amino acid sequence differs from that predicted in Aspergillus genomic databases in amino acids not relevant for catalysis. The enzyme is thermo-alkaline, showing its maximum activity at pH9 and 60°C, and it retains more than 60% of its initial activity after incubation for 1h at 60°C for pH values between 6 and 10. ANCUT2 is more active towards long-chain esters and it hydrolyzes cutin; however, it also hydrolyzes short-chain esters. Cutinase is inhibited by metal ions, PMSF, SDS, and EDTA (10mM). It retains 50% of its activity in most of the solvents tested, although it is more stable in hydrophobic solvents. According to its found biochemical properties, preliminary assays demonstrate its ability to synthesize methyl esters from sesame oil and the most likely application of this enzyme remains in detergent formulations.

Isolation and Screening of Protease Producing Bacteria from Local Environment for Detergent Additive

Proteases are among the most important hydrolytic enzymes that found in every organism to undertake important physiological functions. They are multipurpose enzymes used in various industries such as detergent, silver recovery, food, pharmaceutical, leather, and textile industries. This work aimed to produce protease from indigenous microbes for use as detergent additive. Isolation of protease producer was undertaken using skim milk agar medium. Crude enzyme was characterized in terms of wash and stain removal tests. A total of 188 protease positive bacteria were isolated from seven samples collected from Arba Minch town. Out of 36 alkaline protease producing bacteria, one isolate designated as Bacillus sp. Cab44 was selected. The optimum activity was reached at pH 9 and 50°C. The enzyme was stable in the pH range of 7 to 10. It retained 75%, 86% and 72% activity after one hr pre-incubation at 50°C, in 15% H2O2 and 0.3% commercial detergent respectively. The enzyme activity was increased by Mg2+, Cu2+, and Mn2+, was not affected by Ca2+ but decreased by Zn2+, Hg2+ and Fe2+. It removed stains of blood and egg yolk on cotton cloth at pH 9, 40°C, 5.07 U/ml in 30-40 min. These properties suggest that protease from Bacillus sp. Cab44 could find potential application in detergent industries as good candidate of additive in detergent formulation which have economic implication.

Alternative to Water Based Fabric Cleaner in Textile and Detergent Processes

Three different detergent formulations, (1) ethyl-hydro-oxides (EHOs, using ethanol + H2O2 + KOH + water, without pH adjustment, at 60°C for 1 h), (2) modified EHOs (using ethanol + H2O2 + KOH + water, with pH adjustment, at 40°C for 1 h), and (3) water based detergent (WBD, using commercial detergent T + water, at 40°C for 1 h), were analyzed for cleaning of dried biodiesel soaked cotton cloth (DBSCC) samples. The effects of detergent formulations were analyzed based on cloth sample weights (residual and intact) and visual (through photographic images) examinations. With EHOs formulations, the increasing concentration of KOH and H2O2 had a significant effect on increasing both brightness and residual content of DBSCC samples. On the contrary, the controlled pH environments (as with modified EHOs formulations) had a significant effect in decreasing residual content and increasing brightness of DBSCC samples. The implications of EHOs formulations (with and without modification) are discussed with respect to current water based textile and detergent industries practices.

Catalytic Properties of Amylolytic Enzymes Produced by Gongronella butleri Using Agroindustrial Residues on Solid-State Fermentation.

Amylases catalyze the hydrolysis of starch, a vegetable polysaccharide abundant in nature. These enzymes can be utilized in the production of syrups, alcohol, detergent, pharmaceutical products, and animal feed formulations. The aim of this study was to optimize the production of amylases by the filamentous fungus Gongronella butleri by solid-state fermentation and to evaluate the catalytic properties of the obtained enzymatic extract. The highest amylase production, 63.25 U g−1 (or 6.32 U mL−1), was obtained by culturing the fungus in wheat bran with 55% of initial moisture, cultivated for 96 h at 25°C. The enzyme presented optimum activity at pH 5.0 and 55°C. The amylase produced was stable in a wide pH range (3.5–9.5) and maintained its catalytic activity for 1 h at 40°C. Furthermore, the enzymatic extract hydrolyzed starches from different vegetable sources, presenting predominant dextrinizing activity for all substrates evaluated. However, the presence of glucose was observed in a higher concentration during hydrolysis of corn starch, indicating the synergistic action of endo- and exoamylases, which enables the application of this enzymatic extract to produce syrups from different starch sources.

Development of Bacillus subtilis Mutants for Overproduction of Protease

Proteases are widely used in leather processing, silk industry, diary meat processing, and preparation of organic fertilizer as well as for the liberation of silver from recycled X-ray films. Ultraviolet radiation mutagenesis of Bacillus subtilis IBL-04 was carried out for hyper producing strain development. Mutants of Bacillus subtilis were isolated and screened for selection of hyper producing mutant. Production of protease by the selected mutant BS-90 (treated for 90 min) was optimized by varying pH, temperature, and inoculum size and fermentation time simultaneously in Response Surface Method (RSM) under Central Composite Design (CCD). The mathematical response model is considered to be reliable with an R2 value of 0.9842. The adjusted R2 value was 0.9695 suggesting a significant model by determining the close relationship to the actual R2 value. Predicted R2 value shown in this model was 0.9133. The Pred R-Squared of 0.9133 is close as to the Adj R-Squared of 0.9695 as expected. The ratio of 22.60 attained in this model represents an adequate signal. The calculated C.V was 3.25 which indicate the good level of model precision and reliability. The maximum enzyme activity was 95.89 (IU/mL) at optimum conditions pH 8, Temperature 50°C, Inoculum size 2.5 mL and fermentation time 72 h. These characteristics render its potential use in detergent industries for detergent formulation.

Synthesis, physicochemical, and biological activities of novel N-acyl tyrosine monomeric and Gemini surfactants in single and SDS/CTAB-mixed micellar system

A series of single-chained N-acyl tyrosine surfactants with varying chain lengths (C10-C18) and degree of unsaturation, as well as an N-acyl Gemini tyrosine surfactant with chain length C12, were synthesized, and the structures were confirmed using spectral analysis. The effect of chain length and level of unsaturation on the physicochemical and antibacterial properties of the N-acyl tyrosine surfactants was evaluated. The C12 derivative displayed the optimum antibacterial activity among the single chain surfactants, and the presence of double bond in the oleoyl derivative enhanced the antibacterial activity over its saturated analogue. The N-acyl Gemini surfactant displayed the highest antibacterial activity among the series and also showed greater micelle forming ability than its single chain analogue. Mixed micellar behavior of the N-acyl Gemini surfactant with conventional cationic (CTAB) and anionic (SDS) surfactants in aqueous solution was studied. The negative value of the interaction parameter β12 observed for the N-acyl Gemini in binary mixture with CTAB surfactant indicated a synergistic interaction within the mixed micellar system. However, the binary mixture with SDS displayed antagonistic behavior. The binary mixture of N-acyl Gemini surfactant with CTAB displayed better antibacterial activity and foaming properties than with SDS mixtures. Optimum antibacterial activity was observed for N-acyl Gemini surfactant with mole ratio 0.4 to 0.6 in the CTAB binary mixture, at which the lowest ocular irritation index was observed. Overall, the study showed that the Gemini surfactant in combination with the conventional surfactant CTAB can be used as potential ingredients in detergent and pharmaceutical formulations.

Synthesis and Application of Palm Fatty Acid Distillate Based Alkyd Resin in Liquid Detergent

AbstractPalm fatty acid distillate (PFAD) is the by‐product obtained during physical refining of crude palm oil, which mainly consists of free fatty acids along with minor amounts of glycerides, bioactive compounds such as tocopherols, tocotrienols, phytosterols, squalene, other hydrocarbons. In the present work, an eco‐friendly alkyd resin was prepared using sustainable feedstock such as PFAD along with rosin. The various physico‐chemical properties of PFAD‐based alkyd resin (PFAD‐AR) such as acid value, saponification value, viscosity and volatile matter were determined and compared to palm oil based alkyd resin (PO‐AR). The structural properties of the alkyd resins were investigated using Fourier transform infrared (FTIR) and proton nuclear magnetic resonance (1H NMR) spectroscopic techniques. The study presents the utilization of PFAD‐based alkyd resin with sodium lauryl sulfate (SLS) and sodium lauryl ether sulfate (SLES) in the liquid detergent formulation. The performance properties of the PFAD‐based alkyd resin liquid detergent formulations such as surface tension, wetting power and detergency were comparable with palm oil based alkyd resin liquid detergent formulations and with commercial liquid detergent (CLD). Surface tensions of liquid detergent formulations varied from 20 to 30 mN/m with decrease in concentration. The foaming properties of alkyd resin based liquid detergents are reduced with the increase in the amount of alkyd resin polymer in the formulations. Therefore, it has potential application as a foam reducer in detergent for washing machines.

Application of Silicone Surfactant Along with Hydrocarbon Surfactants to Textile Washing for the Removal of Different Complex Stains

AbstractThe present work reports the application of trisiloxane polyether silicone surfactant to remove various stains along with a range of hydrocarbon (organic) surfactants to investigate whether silicone surfactants offer synergism or antagonism during the cotton fabric cleaning process. Cotton fabric was soiled with red wine, turmeric, permanent marker, acrylic paint, and coffee and washed with the original fabric in aqueous solutions of individual surfactant and blend of surfactants by applying the conventional shaking washing method. The detergency and soil redeposition were determined from the alteration in the surface reflectance of prepared stained fabrics and the original fabric after washing. Surfactants used for the washing were trisiloxane polyether silicone surfactant (AG‐Platinum), sodium dodecyl benzene sulfonate, lauryl alcohol ethoxylate (LA‐10), and nonylphenol ethoxylate (NP‐10) and their blends. In comparison with individual hydrocarbon surfactants, blends of surfactants (with different hydrocarbon to silicone surfactant ratios) dislodged stains (accumulated on the fabric as a result of staining) effectively at shorter time and at lower bath ratio because of superior surface properties. With increasing concentration of surfactant, detergency increased and reached a maximum at the critical micelle concentration (CMC). Silicone surfactant reduced the CMCs of the surfactant blends and provided better detergency at lower concentration. From this study, it was found that silicone surfactant could be successfully introduced into laundry detergent formulations.

Characterization of thermo-solvent stable protease from Halobacillus sp. CJ4 isolated from Chott Eldjerid hypersaline lake in Tunisia.

About 110 newly isolated halophilic and halotolerant bacteria were screened for protease production. A moderately halophilic strain (CJ4), isolated from Chott Eldjerid Hypersaline lake in Tunisia, showed the highest activity on agar plate and was then selected. The biochemical and physiological characterization of the isolate along with the 16S rRNA sequence analysis placed it in the genus Halobacillus. Protease production was maximal at 120 g/L NaCl (2 M) and it started from the post-exponential phase reaching a maximum level at the early decline phase of bacterial growth. Protease activity was optimal at 0.4 M NaCl, pH 9 and 45 °C. It showed an excellent stability over wide ranges of temperatures (30-60 °C), NaCl concentrations (0-5 M), and pH values (5-10), which make it a good candidate for industrial applications at harsh conditions. Crude protease was strongly inhibited by PMSF revealing the dominance of serine proteases. Protease activity exhibited high stability in the presence of several organic solvents and detergent additives. These findings make Halobacillus sp. CJ4 protease with a great interest for many biotechnological applications at high salt or low water content such as peptide synthesis and detergent formulation.

Investigation of the physicochemical and biological properties of proline‐based surfactants in single and mixed surfactant systems

AbstractA series of surfactants derived from l‐Proline, the free amine esters, the ester hydrochlorides and the quaternary ammonium compounds with varying chain lengths (C8–C14) were synthesised. The physicochemical and biological properties were determined in both single and sodium dodecyl sulphate (SDS) mixed systems with a view of enhancing the properties of the individual surfactants as potential ingredients in detergent formulations. The mode of action of the proline surfactants were investigated by their ability to form mixed micelles with the phospholipid 1,2‐dimyristoyl‐sn‐glycero‐3‐phosphatidylcholine (DMPC). The presence of a quaternary ammonium moiety and an increase in alkyl chain length were found to enhance the antibacterial activity of the proline QUAT derivatives. The SDS‐C14 QUAT mixed system displayed good antibacterial activity with optimum activity at mole fractions αQUAT: 0.4 and 0.6. The antibacterial activity of the mixed system was found to be governed by the monomers rather than the micelles. The SDS‐C14 QUAT mixed system also showed moderate irritancy which makes them potential candidates as detergents.

Alkaline proteases from a newly isolated Micromonospora chaiyaphumensis S103: Characterization and application as a detergent additive and for chitin extraction from shrimp shell waste

The present study was undertaken to characterize the extracellular thermostable serine alkaline proteases from newly actinomycete strain Micromonospora chaiyaphumensis S103 and to describe their evaluation in commercial detergents and shrimp waste deproteinization. This proteolytic crude extract was active and stable in alkaline solution. It was extremely stable in the pH range of 5.0–12.0. The optimum pH and temperature were 8.0 and 70°C, respectively, using casein as a substrate. The thermoactivity and thermostability of proteases were enhanced by the addition of 5mM Ca2+. Proteases from S103 were also used for shrimp wastes deproteinization in the process of chitin preparation. The percent of protein removal after 3h hydrolysis at 45°C with an enzyme/substrate ratio of 20U/mg had reached 93%. Furthermore, S103 crude enzyme was stable towards several organic solvents and retained 100% of its original activity after 90days of incubation in the presence of methanol, hexane, acetone, and DMSO. These properties make S103 proteases an ideal choice for application in detergent formulations, chitin production, and enzymatic peptide synthesis.

Evaluation of a novel thermo-alkaline Staphylococcus aureus lipase for application in detergent formulations.

An extracellular lipase of a newly isolated S. aureus strain ALA1 (SAL4) was purified from the optimized culture medium. The SAL4 specific activity determined at 60 °C and pH 12 by using olive oil emulsion or TC4, reached 7215 U/mg and 2484 U/mg, respectively. The 38 NH2-terminal amino acid sequence of the purified enzyme starting with two extra amino acid residues (LK) was similar to known staphylococcal lipase sequences. This novel lipase maintained almost 100% and 75% of its full activity in a pH range of 4.0–12 after a 24 h incubation or after 0.5 h treatment at 70 °C, respectively. Interestingly, SAL4 displayed appreciable stability toward oxidizing agents, anionic and non-ionic surfactants in addition to its compatibility with several commercial detergents. Overall, these interesting characteristics make this new lipase promising for its application in detergent industry.

Coconut oil induced production of a surfactant-compatible lipase from Aspergillus tamarii under submerged fermentation.

Filamentous fungi are efficient producers of lipases. The present study focuses on identification of a potent lipolytic fungus and enhancement of lipase production through optimization of nutritional and cultural conditions under submerged fermentation. Molecular characterization of the fungus by 18S rDNA sequencing revealed its identity as Aspergillus tamarii with 98% homology. Maximum lipase production was noted in mineral salts medium supplemented with coconut oil (2.5%, v/v). A combination of ammonium chloride (2%, w/v) and tryptone (2%, w/v) facilitated maximum lipase production at pH 5 of the production medium. A carbon: nitrogen ratio of 1:4 led to significant (p < 0.00008) increase in the enzyme production in the presence of surfactant cetyltrimethylammonium bromide (0.5%, w/v). Maximum lipase activity (2,32,500 ± 192 U/ml/min) was recorded after 7 days of incubation at 25 °C on a rotary shaker at 120 rpm. A 9.8-fold increase in lipase activity was recorded after optimization of the process parameters. Addition of crude lipase enhanced the oil stain removal activity of a commercially available detergent by 2.2-fold. The current findings suggest the potentiality of this fungal lipase to be used in detergent formulation.

Characterization of a novel protease from Aeribacillus pallidus strain VP3 with potential biotechnological interest

The present study investigates the purification and physico-chemical characterization of an extracellular protease from the Aeribacillus pallidus strain VP3 previously isolated from a geothermal oil-field (Sfax, Tunisia). The maximum protease activity recorded after 22h of incubation at 45°C was 3000U/ml. Pure enzyme, designated as SPVP, was obtained after ammonium sulfate fractionation (40–60%)-dialysis followed by heat-treatment (70°C for 30min) and UNO Q-6 FPLC anion-exchange chromatography. The purified enzyme is a monomer of molecular mass about 29kDa. The sequence of the 25 NH2-terminal residues of SPVP showed a high homology with those of Bacillus proteases. The almost complete inhibition by PMSF and DIFP confirmed that SPVP is a member of serine protease family. Its optima of pH and temperature were pH 10 and 60°C, respectively. Its half-life times at 70 and 80°C were 8 and 4h, respectively. Its catalytic efficiency was higher than those of SAPCG, Alcalase Ultra 2.5L, and Thermolysin type X. SPVP exhibited excellent stability to detergents and wash performance analysis revealed that it could remove blood-stains effectively and high resistance against organic solvents. These properties make SPVP a potential candidate for applications in detergent formulations and non-aqueous peptide biocatalysis.

Optimization of Protease Production from &lt;I&gt;Lysinibacillus fusiformis&lt;/I&gt; F3G5 Isolated from the Fish Gut of &lt;I&gt;Oreochromis mossambicus&lt;/I&gt;

Protease producing bacterium was isolated from the fish gut of Oreochromis mossambicus and identified as Lysinibacillus fusiformis F3G5 by 16S rRNA gene sequencing. The nutritional factors such as carbon sources, nitrogen sources, ionic sources and also environmental parameters such as temperature, pH, sodium chloride were optimized to enhance the yield of protease. Among the carbon sources, fructose (439.27±15.14 U/ml) enhanced enzyme production. Ammonium sulphate (439.27±15.14 U/ml) was found to be the best nitrogen source and Zn 2+ ion (662.70±23.32 U/ml) significantly influenced on enzyme production. Protease production was found to be high at pH 7.0, 40 °C at 0.5% NaCl and the partially purified enzyme was highly active under these environmental conditions. The partially purified enzyme showed more than 60% activity in the presence of a few detergents. The demonstrated detergent stability of protease from L. fusiformis F3G5 infers that the enzyme has good compatibility with ingredients present in detergent formulation.

Revealing Detergent Efficiency and Mechanism by Real-Time Measurement Using a Novel and Tailored QCM-D methodology

Abstract Currently there is a lack of knowledge on how to scientifically and rapidly screen new detergent formulations. To address this, we employed the Quartz Crystal Microbalance with Dissipation technique which allows real-time acquisition of the cleaning process. Using an automated multichannel setup enabled rapid, simultaneous screening of eight formulations in regard to cleaning rate, soil swelling and soil removal. Herein, 9 commercially available dishwashing formulations are screened and ranked based on their ability to remove/swell standardized cooking grease soiled onto a silica surface. Moreover, we observed that soil swelling can be monitored via the dissipation factor. In summary, we present a real-time in-situ method for detergent formulation screening during the R&amp;D phase of new detergents.

Effects of Relevant Detergent Components on the Cleaning Performance in Low Temperature Electric Household Dishwashing

Abstract Lowering water temperatures in the cleaning step of a dishwashing program to 30°C leads to reduced energy consumption and decreased cleaning performances on persistently soiled dish- and cookware and of fatty soilings on hydrophobic surfaces. This study focusses on the question if the observed decline of the cleaning performance can be compensated for by aligning the formulation of the dishwashing detergent. A Design of experiments-method is used to quantify the effects of detergent components on the cleaning performance in mathematical models. The calculated models are used to adjust the amount of those components in a detergent formulation that increases the cleaning performance in low temperature electric household dishwashing. The modeled formulation has been verified in practical experiments.

Deterjensi Dari Sagu dan Asam Alginat Terdikarboksilasi yang Biodegradabel

Sago and alginic acid were partially-dicarboxylated and used as an alternative for substitution of sodium tripolyphosphate (STPP) which cause eutrophication in water body. Dicarboxylated sago and alginic acid (ST and AT) with degree of dicarboxylations from 10 to 81 mol% were prepared, and their builder performance in detergent formulation (as relative detergency and calcium ion sequestration capacity), and biodegradabbility were measured. The detergency and calcium ion sequestration capacity of ST and AT depended on the degree of dicarboxylation. AT with degree of dicarboxylations more than 58-60 mol% showed excellent builder performance in detergent formulations based on the detergency and calcium ion sequestration capacity. On the other hand, ST with degree of dicarboxylations more than 25 mol% showed better in biodegradability than AT at the same basis. However, AT with degree of dicarboxylations more than 50 mol% was resistent to biodegradation

Lipase of Bacillus stratosphericus L1: Cloning, expression and characterization

Present work was undertaken to discover new lipolytic enzymes as well as novel bacterial strains for applications in biotechnology. One of the isolated strains identified as Bacillus stratosphericus L1 produced extracellular lipase (LipBST) which was cloned and expressed in Escherichia coli. Purified mature enzyme had a molecular mass of 19kDa. Recombinant protein showed an activity of 6244.5U/mg at pH 9, 35°C. It was stable in the range of 35–55°C and retained more than 60% activity after incubation for 4h. LipBST was activated by organic solvents such as acetone and n-hexane. Lipase was inactivated by all investigated metal ions, inhibitors and detergents. LipBST was determined to be short-chain specific, but also hydrolyzed medium-, long-chain p-nitrophenyl and natural fatty substrates. The values of Vmax and KM for p-nitrophenyl butyrate, p-nitrophenyl caprylate, p-nitrophenyl decanoate were 1.1, 2.5, 0.1mMmin−1 and 5×10−2, 3.4×10−2, 194×10−2mM, respectively. Biochemical characteristics of LipBST suggest a great potential for various biotechnological applications including detergent formulation, bioremediation and organic synthesis processes.