Detergent Preparations Research Articles

Purification and characterization of lipase from a new strain Staphylococcus argenteus MG2 (MTCC 12820)

The lipase enzyme was isolated and purified from Staphylococcus argenteus MG2 (MTCC 12820) to homogeneity using ammonium sulphate precipitation followed by chromatographic techniques. This process resulted in a purification factor of 40.96-fold and a 26.25% recovery with a specific activity of 744.68 U mg-1. The molecular weight of the purified lipase was determined by SDS-PAGE to be 45 kDa. The Km and Vmax values of the purified lipase were calculated to be 4.95 mM and 79.36 µmol/min/mg-1, respectively. The maximum lipase activity was observed at pH 7.0 and 30 ºC with 100% stability, and it was also found to be stable in a broad range of pH (5-12) and temperature (30-90 ºC). The enzymatic activity of this Staphylococcal lipase was increased by Ca2+ to 105.71% at a concentration of 1 mM CaCl2. Additionally, it exhibited marked stability and activity in organic solvents. In the presence of 1% SDS surfactant, it retained 85.16% residual activity, while the metal chelator EDTA (inhibitor) reduced the lipase activity to 83.87% residual activity at a concentration of 1% w/v. This alkali-stable and thermo-stable lipase can be exploited by extending its use in the preparation of detergents and in various industrial and biotechnological applications.

The Genus Allochrusa: A Comprehensive Review of Botany, Traditional Uses, Phytochemistry, and Biological Activities

The genus Allochrusa (Caryophyllaceae) comprises nine species, which are native to Central Asia, Turkey, Iran, Afghanistan, and the Caucasus. They have been used in folk medicine and in the preparation of various sweets and detergents, especially in Asian countries. A diversity of secondary metabolites has been reported from the genus Allochrusa, including triterpene glycosides, ecdysteroids, flavonoids, volatile compounds, fatty acids, polysaccharides, pectins, hemicelluloses, and other phytochemicals. In vitro and in vivo pharmacological studies on isolated compound fractions and extracts from Allochrusa species showed anti-inflammatory, adjuvant, hemolytic, cytotoxic, antifungal, analgesic, antioxidant, and other activities. In this review, the chemical compounds and diverse biological activities of the Allochrusa genus are summarized.

Preparasi Detergen Penyuci Najis Air Liur Anjing dengan Variasi Konsentrasi Surfaktan Metil Ester Sulfonat (MES)

The kaolin detergent preparation as an alternative a dog saliva cleanser has been carried out by varying the concentration of Methyl Ester Sulfonate (MES) surfactant. This study aims to obtain the best kaolin detergent composition based on the results of physicochemical testing. The manufacture of kaolin detergent in this study has three stages. The first step is the preparation and characterization of kaolin using X-Ray Diffraction (XRD). The second step is the manufacture of kaolin detergent with various concentrations of MES surfactant by 10%, 14%, and 18% (w/w). The third step is testing the physicochemical properties which include organoleptic, pH, foam stability, and surface tension. The results showed that kaolin used in the manufacture of detergents has the main mineral content in the form of kaolinite is shown at 2θ=12,24o (d=7,24 Å) and 2θ=24,78o (d=3,58 Å). Based on the results of physicochemical testing, kaolin detergent F3 (MES 18%) was chosen as the best kaolin detergent because it has a thick and homogeneous liquid form, soft texture, white color, has a coconut milk smell, pH 8,270, and surface tension of 0,010 Nm-1.

Combinatorial synthesis enables scalable designer detergents for membrane protein studies.

Non-ionic detergents with tailor-made properties are indispensable tools for today's world applications, such as cleaning, disinfection, and drug discovery. To facilitate their challenging production, herein we introduce a new detergent class, namely scalable hybrid detergents. We report a combinatorial synthesis strategy that allows us to fuse head groups of different detergents into hybrid detergents with unbeatable ease. Importantly, combinatorial synthesis also enables the choice between (i) high-throughput preparation of detergents for small scale applications and (ii) large scale preparation of individual detergents. This combinatorial synthesis strategy enables an unprecedented fine tuning of detergent properties, such as overall polarity and shape, which are determining factors in applications, such as membrane protein research. Our data show that membrane protein purification parameters, such as protein yields and activity, can be linked to overall polarity and shape. Conveniently, both parameters can be theoretically described by means of the hydrophilic–lipophilic balance (HLB) and packing parameter concepts. Both concepts are principally applicable to all non-ionic detergent classes, which facilitates the identification of widely applicable design guidelines for the predictable optimization of non-ionic detergents. Our findings permit access to a yet unexplored chemical space of the detergentome, therefore creating new possibilities for structure–property relationship studies. Seen from a broader perspective, combinatorial synthesis will facilitate the preparation of designer detergents with tailor-made properties for future applications in today's world.

Pelatihan Pembuatan Eco-Friendly Detergen Daun Balik Angin (Alphitonia Excelsa) pada Kelompok Ibu-ibu di Desa Mandi Angin

Special Purpose Forest Area (KHDTK) Lambung Mangkurat University is a forest area with types of plants and trees. KHDTK is close to residential areas. The existence of community activities around KHDTK will indirectly have an impact on the sustainability of KHDTK. The community activities that impact KHDTK are bathing, washing, and latrine activities (MCK). This community activity provides insight into the impact of using chemical detergents on health and the environment, as well as increasing community empowerment around the KHDTK area in processing natural resources in the form of processing leaves into environmentally friendly detergents. The implementation method consists of two steps, the first step is counseling, and the second step is the preparation of eco-friendly detergents. Counseling carried out by providing knowledge about the impact of synthetic detergents and the manufacture of environmentally friendly detergents. In this activity, the active ingredients used are balik angin leaves because these leaves contain saponins. Leaves balik angin extraction using the infusion method. The results of the evaluation of the activities showed an increase in public knowledge about the impact of synthetic detergents on the environment and an increase in community skills in making environmentally friendly detergents. This activity is very useful in increasing the knowledge and skills of the community.

Application of Benzol Sulfonates in the Preparation of Detergents

In this article the usage of alkilbenzene is considered as a washinh facility. This scientific article also suggests the most cost-effective and inexpensive way to make soap. Household detergents can be solid, liquid or powder, detergents in powder form differ from liquid form not only in physical form but also in the proportions of its components, the amount of surfactants is higher than in powder form, liquid detergents studies of spatial separation observation during long-term storage are presented. The article also discusses the study of the addition of surfactants from detergents to improve the washing properties of soap, as well as reduce its absorption, as well as the reduction of the cost of soap due to the addition of clay from local raw material

Nanobioremediation: A sustainable approach towards the degradation of sodium dodecyl sulfate in the environment and simulated conditions.

Nanotechnology has gained huge importance in the field of environmental clean-up today. Due to their remarkable and unique properties, it has shown potential application for the remediation of several pesticides and textile dyes. Recently it has shown positive results for the remediation of sodium dodecyl sulfate (SDS). One of the highly exploited surfactants in detergent preparation is anionic surfactants. The SDS selected for the present study is an example of anionic linear alkyl sulfate. It is utilized extensively in industrial washing, which results in the high effluent level of this contaminant and ubiquitously toxic to the environment. The present review is based on the research depicting the adverse effects of SDS in general and possible strategies to minimizing its effects by bacterial degradation which are capable of exploiting the SDS as an only source of carbon. Moreover, it has also highlighted that how nanotechnology can play a role in the remediation of such recalcitrant pesticides.

A LITERARY REVIEW ON SAPINDUS TRIFOLIATUS (GASPENELA) AND ITS MEDICINAL VALUES

Sapindus trifoliatus is a large tree used in treatment of numerous ailments. Its fruits, known as soap nuts, contain Saponin and are widely used in cosmetics. Fruits, skin of the fruit, seeds and leaves are used in medicine internally and externally. Knowledge on medicinal uses of Sapindus trifoliatus is scattered. Therefore, it was decided to gather and record this dispersed information. Data was collected from Ayurveda and Sri Lankan medical books, journals, physicians and through web search. Sapindus trifoliatus is used to conduct Vamana Karma, Virechana Karma and Nasya Karma. It is used in treatment of migraine, epilepsy, bronchial asthma, cough and burning sensation. It is also used in preparation of body shampoo, hair shampoo and detergents. Anti- ulcer, anthelmintic, anti-inflammatory, muscle relaxant, anti-acne and anti-dandruff effect of Sapindus trifoliatus is scientifically proven. Leaf extract was found to be non-toxic up to 2g/kg but frequent administration in high doses elevate in aspartate aminotransferase, alanine aminotransferase, blood urea and serum creatinine in rats. It is concluded that Sapindus trifoliatus has multifaceted medicinal values.

Highly β-Selective Glycosylation Reactions for the Synthesis of ω-Functionalized Alkyl β-Maltoside as a Co-crystallizing Detergent

Methods have been reported for the preparation of ω-functionalized alkyl maltoside and glycoside detergents via a simple and inexpensive synthetic route. The key step was stannic chloride-mediated glycosylation of long-chain alcohols or thiols with maltose octaacetate at 0 or –10°C, respectively, within a very short time (isolated yield 17–44%), which provided more than 98% β-selectivity.

Enhancement of Characteristics and Potential Applications of Amylases: A Brief Review

Starch is the major storage carbohydrate of plant products. Amylases are the group of enzymes hydrolyzes starch and related polymers to smaller oligosaccharides and less amount of monosaccharide. Microbes are the major sources of amylases, exploited for large scale production in different industries. Recently, protein engineering has been applied to improve the structural and physicochemical properties of the enzyme for its potential applications. Amylases are mostly used for liquefaction of starch in the purpose of glucose, maltose, and high fructose containing syrup preparation, malto-oligosaccharides production, desizing, production of bio-fuel, detergent preparation, waste management, and preparation of digestive aids.

De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.

Membrane proteins perform many important cellular functions. Historically, structural studies of these proteins have been conducted in detergent preparations and synthetic lipid bilayers. More recently, magic-angle-spinning (MAS) solid-state NMR has been employed to analyze membrane proteins in native membrane environments, but resonance assignments with this technique remain challenging due to limited spectral resolution and high resonance degeneracy. To tackle this issue, we combine reverse labeling of amino acids, frequency-selective dipolar dephasing, and NMR difference spectroscopy. These methods have resulted in nearly complete resonance assignments of the transmembrane domain of human LR11 (SorLA) protein in E. coli membranes. To reduce background signals from E. coli lipids and proteins and improve spectral sensitivity, we effectively utilize amylose affinity chromatography to prepare membrane vesicles when MBP is included as a fusion partner in the expression construct.

Quality and Detergency Optimization, Liquid Detergent Preparation, Mahogany Seed Extract (Swietenia mahagoni)

The use of <em>Linear Alkylbenzene Sulfonate</em>(LAS) as a surfactant for making detergent can pollute aquatic ecosystem and agricultural soils. Mahogany seed extract can be used as a substitute for LAS because it contains saponin so that it can be used also as a foaming agent to remove dirt on clothes. This research aims to know the optimum liquid detergent formula seen from its suitability with SNI 06-4075-1996 about Liquid Washing Detergents, foam stability and detergency power. The research steps are (1) Making simplicia (2) Extracting mahogany seeds with ethanol solvent (3) Identification of saponin (4) Making liquid detergent preparations (5) Quality test, foam stability test and detergency power. The results showed that formula 2 with a ratio of mahogany seed extract : LAS is 2 : 1 is the most optimum formula because it appropiate with SNI, and has the best foam stability and detergency power. Formula 2 has pH 11.1; specific gravity 1.1; 0.1% free alkaline, foam stability of 70% and detergency without rinsing 91.53% and by rinsing 94.680%.<pre><em> </em></pre>

Detergent-compatible bacterial cellulases.

Cellulases, lipases, proteases, and amylases are employed in the detergent preparation to speed up the detergency process. Microbial cellulases are now commercially manufactured and are being used by various industries like detergent industry. Currently, the supplementation of detergent-compatible enzymes is a new trend followed by most of the detergent industries. The cellulases are supplemented to the detergents to improve the fabric smoothness and soil removal without damaging them. They act by passing through the textile interfibril spaces and thus the fabric quality is preserved. The process is environment friendly, and the use of cellulases and other detergent-compatible enzymes diminishes the utilization of toxic detergent constituents that are hazardous to humans. Alkaline cellulases active at ambient and low temperature are now preferred to maintain the fabric quality and use of low energy. The review reports on the production, purification, and properties studies of detergent-compatible proteases, amylases, and lipases are available. However, there is no report on detergent-compatible bacterial cellulases. In the present review, an overview on the production, purification, and characterization of detergent bacterial cellulases is presented. The stability and compatibility of the alkaline bacterial cellulases in the presence of the detergents and the detergent constituents are also discussed.

Generation of membrane proteins in polymer-based lipoparticles as flow cytometry antigens

A major obstacle in the study of membrane proteins is the challenge in generating purified targets in a stable and native conformation. Potentially destabilizing detergents are often used to extract targets out of their native membranes. One approach to overcome these destabilization issues is to present targets in a lipid bilayer environment. While numerous lipid bilayer presentation approaches such as Nanodiscs and liposomes have been used through the years, most still require a detergent purified protein intermediate. Styrene-maleic acid lipoparticles (SMALPs) have been developed to directly solubilize membranes without the use of detergents and present membrane proteins in a native lipid bilayer environment. These discoidal lipid bilayer particles have been evaluated on several membrane protein classes (e.g. ion channels, transporters) and applications (e.g. spectroscopy, electron microscopy). Here, cannabinoid receptor 1 (CB1), a class A G-protein coupled receptor, was incorporated into a SMALP (CB1-SMALP) and shown to retain its native fold through binding studies with a CB1-specific conformational antibody. The binding studies were conducted in yeast and mammalian display formats using fluorescence-activated cell sorting (FACS). Compared to detergent preparations, CB1-SMALP also exhibited a marked increase in thermostability. This study provides the framework for a platform to generate full-length membrane protein screening antigens for flow cytometry-based studies.

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

AbstractCurrently, 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.

Biochemical properties of the alkaline lipase of Bacillus flexus XJU-1 and its detergent compatibility

The possibility of using Bacillus flexus XJU-1 lipase in detergent preparations was studied. The enzyme was monomeric protein as confirmed by liquid chromatography-mass spectrometry and its molecular weight was 15.95 kDa. The lipase showed optimum activity at pH 10.0 and was 100% stable for 24 h at pH 10.0 and 11.0. It exhibited maximum activity at 70°C and retained more than 70% of the initial activity at 60, 70 and 80°C for 24 h. The activity was stimulated by Ca2+, Ba2+, Mg2+ and Co2+, whereas 50% of the initial activity was lost with Fe3+ and Hg2+. The activity was inhibited by 10 mM N-bromosuccinimide and tosyl-L-lysylchloromethylketone, while N-ethylmaleimide, phenylmethylsulphonylfluoride and urea did not show any effect. The enzyme significantly hydrolysed olive, cottonseed, sunflower, groundnut, and gingelly oils. With p-nitrophenyl palmitate, Vmax and Km were 62.5 U/mL and 2.25 mM, respectively. The lipase maintained its stability in Tween-80, Triton-100 and H2O2 at 1%, but an activation of 10% and a reduction of 15% in relative activity were observed with NaClO and sodium dodecyl sulphate, respectively. The enzyme retained maximum storage stability for 20 days at −20, 4 and 30°C. In the presence of 0.7% (w/v) Ariel, Henko, Super wheel, Tide plus and Rin, a retention of more than 84.90% initial activity was recorded after 24 h at 60°C. The supplementation of the lipase to the detergents improved the olive oil stain removal. These properties suggested the present enzyme as a potential additive for detergent preparations.

Cryo-EM Studies of RyR1 Channel in Detergent-Free Aqueous Environment

Skeletal muscle ryanodine receptor (RyR1) is a Ca2+ release channel in the sarcoplasmic reticulum membrane and plays a key role in excitation-contraction coupling. Obtaining high-resolution 3D structure of RyR1 is a formidable challenge due to its enormous size (∼2.3 MDa), dynamic nature and location in the lipid membrane in native state. Detergents are traditionally used to make membrane proteins water soluble and suitable for single-particle cryo-EM. However, detergents tend to destabilize and inactivate membrane proteins. In addition, the presence of detergent in the protein sample reduces surface tension of water making it difficult to control the ice thickness and distribution of channel particles in cryospecimen, and leads to low-contrast in cryo-images. To overcome these difficulties we used amphipathic polymer, amphipol 8-35 (APol8-35), to substitute for detergent in RyR1 preparations. We tested functionality of RyR1/APol8-35 in a [3H]ryanodine binding assay, which yielded Kd and Bmax values similar to those of the purified RyR1 in the presence of CHAPS, indicating that the high-affinity binding site for ryanodine is retained in RyR1/APol8-35. The use of Apol8-35 allowed us to reproducibly obtain ice-embedded specimens of RyR1 for cryo-EM analysis and resulted in improved ice thickness with channel particles uniformly distributed across the holes in the grids. The protein contrast of ice-embedded RyR1/APol8-35 is substantially higher than in detergent preparations using a traditional CCD detector. Furthermore, low-dose images of vitrified RyR1/APol8-35 have been collected on the DE-12 back-thinned DDD camera using JEM3200FSC electron cryomicrosope operated at 300 keV at liquid nitrogen temperature. Preliminary analysis of these cryo-EM images demonstrates image signals that extend beyond ∼6A. Optimal conditions for both sample vitrification and data acquisition were reached in order to achieve a higher resolution RyR1 structure. Supported by NIH (R21AR063255, R01GM072804, R01GM080139, P41GM103832) and AHA (12GRNT10510002).

From structure to catalysis: recent developments in the biotechnological applications of lipases.

Microbial lipases are highly appreciated as biocatalysts due to their peculiar characteristics such as the ability to utilize a wide range of substrates, high activity and stability in organic solvents, and regio- and/or enantioselectivity. These enzymes are currently being applied in a variety of biotechnological processes, including detergent preparation, cosmetics and paper production, food processing, biodiesel and biopolymer synthesis, and the biocatalytic resolution of pharmaceutical derivatives, esters, and amino acids. However, in certain segments of industry, the use of lipases is still limited by their high cost. Thus, there is a great interest in obtaining low-cost, highly active, and stable lipases that can be applied in several different industrial branches. Currently, the design of specific enzymes for each type of process has been used as an important tool to address the limitations of natural enzymes. Nowadays, it is possible to “order” a “customized” enzyme that has ideal properties for the development of the desired bioprocess. This review aims to compile recent advances in the biotechnological application of lipases focusing on various methods of enzyme improvement, such as protein engineering (directed evolution and rational design), as well as the use of structural data for rational modification of lipases in order to create higher active and selective biocatalysts.

Universal Phase Transformation Mechanism and Substituted Alkyl Length and Number Effect for the Preparation of Overbased Detergents Based on Calcium Alkylbenzene Sulfonates

Overbased calcium sulfonate is one of the largest commercially produced nanomaterials; the phase transformation mechanism involved in the key process of carbonation reaction for overbased detergent preparation has not yet been fully understood. Following our previous investigation based on the heavy alkylbenzene sulfonate (HABS) surfactant of industrial byproduct, two commercial products with well-defined chemical compositions and structures, long-chain alkylbenzene sulfonate (LCABS) and comparative short-chain linear alkylbenzene sulfonate (SLABS), are employed in this study as model surfactants for further mechanism study of this pivotal process by the combination of analytical techniques such as potentiometric titration, DLS, TEM, FTIR, and XRD. It has been demonstrated that amorphous calcium carbonate (ACC) is a prerequisite for the preserving and stabilization of the alkaline reserve, especially under thermal work environment. The phase transformation from ACC to crystalline vaterite polymorph rather...

Chromosomal Integration에 의해 제조한 Bacillus clausii C5 유래의 alkaline protease의 세제 첨가제 응용성

Bacillus clausii I-52 which produced SDS- and H₂O₂-tolerant extracellular alkaline protease (BCAP) was isolated from heavily polluted tidal mud flat of West Sea in Incheon, Korea and stable strain (transformant C5) of B. clausii I-52 harboring another copy of BCAP gene in the chromosome was developed using the chromosome integration vector, pHPS9-fuBCAP. When investigated the production of BCAP using B. clausii transformant C5 through pilot-scale submerged fermentation (500 L) at 37℃ for 30 h with an aeration rate of 1 vvm and agitation rate of 250 rpm, protease yield of approximately 105,700 U/mL was achieved using an optimized medium (soybean meal 2%, wheat flour 1%, sodium citrate 0.5%, K₂HPO₄ 0.4%, Na₂HPO₄ 0.1%, NaCl 0.4%, MgSO₄ · 7H₂O 0.01%, FeSO₄· 7H₂O 0.05%, liquid maltose 2.5%, Na₂CO₃ 0.6%). The enzyme stability of BCAP was increased by addition of polyols (10%, v/v) and also, the stabilities of BCAP towards not only the thermal-induced inactivation at 50℃ but also the SDS and H₂O₂-induced inactivation at 50℃ were enhanced. Among the polyols examined, the best result was obtained with propylene glycol (10%, v/v). The BCAP supplemented with propylene glycol exhibited extreme stability against not only the detergent components such as α-orephin sulfonate (AOS) and zeolite but also the commercial detergent preparations. The granulized enzyme of BCAP was prepared with approximately 1,310,000 U/g of granule. Wash performance analysis using EMPA test fabrics revealed that BCAP granule exhibited high efficiency for removal of protein stains in the presence of anionic surfactants as well as bleaching agents. When compared to Savinase 6T ⓡ and Everlase 6T ⓡ manufactured by Novozymes, BCAP under this study probably showed similar or higher efficiency for the removal of protein stains. These results suggest that the alkaline protease produced from B. clausii transformant C5 showing high stability against detergents and high wash performance has significant potential and a promising candidate for use as a detergent additive.