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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 (LC 50 of 11.3 mg/L).

A novel extracellular lipase from a filamentous fungus Ascomycota strain, P22, was isolated from olive mill wastewater, then purified and characterized. This strain was identified as Penicillium crustosum Thom based on sequencing analyses. Penicillium crustosum Thom strain P22 lipase (PCrL) was purified 63-fold to homogeneity using ammonium sulfate precipitation and chromatography on a Q-Sepharose Fast Flow column, with a total yield of 34%. The purified PCrL had a molecular mass of 28 kDa, estimated by SDS-PAGE. The 20 NH2-terminal amino-acid residues showed a high degree of homology with those of other Penicillium lipases. The specific activity of PCrL at pH 9 and 37 °C were found to be 5000 and 10,000 U/mg on olive oil and trioctanoin emulsions, respectively. PCrL exhibited clear regioselectivity toward the sn-1 position of the surface-coated triglycerides which were esterified with α-eleostearic acid at the sn-1/3 position. PCrL was completely inhibited by 53 µM of Orlistat, 5 mM of phenylmethylsulfonylfluoride, and 2 mM of diiodopropyl fluorophosphate, suggesting that it belonged to the serine lipase family. PCrL showed high activity and stability in the presence of water-immiscible organic solvents, surfactant, and oxidizing agents, and showed considerable compatibility with commercial laundry detergents. Washing performance analysis revealed that it could effectively remove oil stains. Hence, PCrL has several attractive properties that make it a promising potential candidate for detergent formulations.

Bacterial lipases with activity spanning over a broad temperature and substrate range have several industrial applications. An efficient enzyme-producing bacterium Chryseobacterium polytrichastri ERMR1:04, previously reported from Sikkim Himalaya, was explored for purification and characterization of cold-adapted lipase. Optimum lipase production was observed in 1% (v/v) rice bran oil, pH 7 at 20°C. Size exclusion and hydrophobic interaction chromatography purified the enzyme up to 21.3-fold predicting it to be a hexameric protein of 250 kDa, with 39.8 kDa monomeric unit. MALDI-TOF-MS analysis of the purified lipase showed maximum similarity with alpha/beta hydrolase (lipase superfamily). Biochemical characterization of the purified enzyme revealed optimum pH (8.0), temperature (37°C) and activity over a temperature range of 5–65°C. The tested metals (except Cu2+ and Fe2+) enhanced the enzyme activity and it was tolerant to 5% (v/v) methanol and isopropanol. The Km and Vmax values were determined as 0.104 mM and 3.58 U/mg, respectively for p -nitrophenyl palmitate. Bioinformatics analysis also supported in vitro findings by predicting enzyme's broad temperature and substrate specificity. The compatibility of the purified lipase with regular commercial detergents, coupled with its versatile temperature and substrate range, renders the given enzyme a promising biocatalyst for potential detergent formulations.

Lipase is an important commercial enzyme with unique and versatile biotechnological applications. This study was conducted to biosynthesize and characterizes alkaliphilic lipase by Exiguobacterium sp. strain AMBL-20T isolated from the glacial water samples of the northeastern (Gilgit-Baltistan) region of Pakistan. The isolated bacterium was identified as Exiguobaterium sp. strain AMBL-20T on the basis of morphological, biochemical, and phylogenetic analysis of 16S rRNA sequences with GenBank accession number MW229267. The bacterial strain was further screened for its lipolytic activity, biosynthesis, and characterization by different parameters with the aim of maximizing lipase activity. Results showed that 2% Olive oil, 0.2% peptone at 25 °C, pH 8, and 24 h of incubation time found optimal for maximum lipase production. The lipase enzyme was partially purified by ammonium sulphate precipitation and its activity was standardized at pH 8 under 30 °C temperature. The enzyme showed functional stability over a range of temperature and pH. Hence, extracellular alkaliphilic lipase from Exiguobacterium sp. is a potential candidate with extraordinary industrial applications, particularly in bio-detergent formulations.

A novel alkaline serine protease, derived from the Staphylococcus aureus strain ALA1 previously isolated from dromedary milk, was subjected to purification and characterization. Optimal protease production occurred under specific culture conditions. The purified protease, designated S. aureus Pr with a molecular mass of 23,662 Da and an N-terminal sequence, showed an approximately 89% similar identity with those of other Staphylococcus strains. It exhibited its highest enzymatic activity at a pH of 10.0 and 60 °C in the presence of 3 mM Ca2+. Remarkable thermostability was observed at temperatures up to 70 °C and within a pH range of 6.0 to 10.0 for 2 h. The presence of Ca2+ or Mg2+ and Zn2+ significantly enhanced both enzymatic activity and thermal stability. Additionally, notable stability was demonstrated in the presence of reducing and chaotropic agents as well as in surfactants, oxidizing agents, and organic solvents commonly found in detergent compositions. This highlights the enzyme’s potential as a versatile biocatalyst, especially in detergents. Its stability and compatibility with laundry detergents matched Alcalase 2.5 L, type Dx, and the Stearothermophilus protease, used as controls. Collectively, this study investigated the potential utilization of S. aureus Pr in industrial detergents as an excellent candidate for incorporation as an additive in detergent formulations.

Dump sites harbour microorganisms with potential for environmentally friendly industrial applications. This study assessed the lipolytic activity of municipal dumpsite-associated bacteria and evaluated the stability of the most potent isolate’s lipolytic enzyme against laundry detergents. It also examined the crude lipase’s ability to remove stains from cotton fabric. Among twelve bacteria isolated, five demonstrated notable halo zones on tributyrin agar plates. The diameters (mm) were MN38 (11 ± 1.4), MN1310 (8.5 ± 0.7), MN28 (6.5 ± 0.71), MN18 (7.0 ± 1.4), and MN310 (8.15 ± 0.21). Quantitative analysis revealed that MN38 exhibited the highest lipase activity (14.76 ± 0.27 U/mL), while MN1310 showed the lowest (6.40 ± 0.85 U/mL). Nucleotide sequence analysis identified the isolates as Raoultella terrigena veli18 (MN38), Stenotrophomonas maltophilia veli96 (MN1310), Viridibacillus sp. veli10 (MN28), Stenotrophomonas sp. veli19 (MN18), and Klebsiella sp. veli70 (MN310). The crude lipase from R. terrigena veli18 maintained 73.33%, 52.67%, 55.0%, and 54.0% of its original activity after 60 min of exposure to Sunlight, Surf, Maq, and Omo, respectively. Adding crude lipase to enzyme-free laundry detergents significantly enhanced their cleaning efficacy, completely removing oil stains from cotton fabric. This performance of R. terrigena veli18 crude lipase highlights its potential as an effective detergent bio-additive.

Background Proteases are hydrolytic enzymes that catalyze peptide linkage cleavage reactions at the level of proteins and peptides with different degrees of specificity. This group draws the attention of industry. More than one protease in three is a serine protease. Classically, they are active at neutral to alkaline pH. The serine proteases are researched for industrial uses, especially detergents. They are the most commercially available enzyme group in the world market. Overall, fungi produced extracellular proteases, easily separated from mycelium by filtration. Results A new basidiomycete fungus CTM10057, a hyperproducer of a novel protease (10,500 U/mL), was identified as Pleurotus sajor-caju (oyster mushroom). The enzyme, called SPPS, was purified to homogeneity by heat-treatment (80 °C for 20 min) followed by ammonium sulfate precipitation (35–55%)-dialysis, then UNO Q-6 FPLC ion-exchange chromatography and finally HPLC-ZORBAX PSM 300 HPSEC gel filtration chromatography, and submitted to biochemical characterization assays. The molecular mass was estimated to be 65 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Native-PAGE, casein-zymography, and size exclusion by HPLC. A high homology with mushroom proteases was displayed by the first 26 amino-acid residues of the NH 2 -terminal aminoacid sequence. Phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP) strongly inhibit SPPS, revealing that it is a member of the serine-proteases family. The pH and temperature optima were 9.5 and 70 °C, respectively. Interestingly, SPPS possesses the most elevated hydrolysis level and catalytic efficiency in comparison with SPTC, Flavourzyme® 500 L, and Thermolysin type X proteases. More remarkably, a high tolerance towards organic solvent tolerance was exhibited by SPPS, together with considerable detergent stability compared to the commercial proteases Thermolysin type X and Flavourzyme® 500 L, respectively. Conclusions This proves the excellent proprieties characterizing SPPS, making it a potential candidate for industrial applications especially detergent formulations.

The encapsulation of bioactive agents through the utilization of biodegradable nanoparticles is a topic of considerable scientific interest. In this study, microcapsules composed of chitosan (CS) and Arabic gum (GA) nanoparticles were synthesized, encapsulating oregano essential oil (OEO) through Pickering emulsions and subsequent spray drying. The optimization of hybrid chitosan and Arabic gum (CS–GA) nanoparticle formation was carried out via complex coacervation, followed by an assessment of their behavior during the formation of the emulsion. Measurements of the size, contact angle, and interfacial tension of the formed complexes were conducted to facilitate the development of Pickering emulsions for encapsulating the oil under the most favorable conditions. The chitosan–Arabic gum capsules were physically characterized using scanning electron microscopy and fitted to the Beerkan estimation of soil transfer (BEST) model to determine their size distribution. Finally, the OEO encapsulation efficiency was also determined. The optimum scenario was achieved with the CS–GA 1–2 capsules at a concentration of 2% wt, featuring a contact angle of 89.1 degrees, which is ideal for the formation of oil/water (O/W) emulsions. Capsules of approximately 2.5 μm were obtained, accompanied by an encapsulation efficiency of approximately 60%. In addition, the hybrid nanoparticles that were obtained showed high biodegradability. The data within our study will contribute fundamental insights into CS–GA nanoparticles, and the quantitatively analyzed outcomes presented in this study will hold utility for forthcoming applications in environmentally friendly detergent formulations.

Lipases are hydrolytic enzymes owing much importance in industrial applications. These enzyme-based detergents are ecofriendly and produce a wastewater with low level of COD (chemical oxygen demand). In the present work, a novel halophilous, thermoalkaline, and detergent-tolerant lipase produced by a newly isolated Aeribacillus pallidus strain VP3 was studied. Considerable interest has been given to this lipase by the improvement of its catalytic activity through the optimization of the pH, the (C/N) ratio, and the inoculum size, using the response surface methodology based on the Box-Behnken design of experiments. A total of 16 experiments were conducted, and the optimized pH, (C/N) ratio, and inoculum size were 10, 1, and 0.3, respectively. The results of the analysis of variance (ANOVA) test indicated that the established model was significant ( p value < 0.05). The optimization of the production conditions leads to 2.83-fold of increase in the catalytic activity calculated as the ratio of the activity obtained after optimization (68 U) and the initial activity before optimization (24 U). All in all, the lipase of Aeribacillus pallidus could be considered as a potential candidate to be incorporated in detergent formulations since it shows a good stability towards detergents and wash performance.

It is commonly known that cationic and anionic surfactants cannot be mixed without the risk of precipitation or instability. However, many studies have shown that not only is it possible to combine cationic and anionic surfactants, but also that this combination can present synergic properties. Mixtures of anionic and cationic surfactants have many unique properties that can be very useful when used properly. The aim of this report is to present relevant information concerning the interaction between anionic and cationic surfactants. A bibliographic review on anionic/cationic mixtures is presented here in order to better understand their properties and possible synergic effects, as this is of practical importance for the chemical industry.