TABLE 7 - uploaded by Hans Sejr Olsen
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Enzymes have effectively assisted the development and improvement of modern household and industrial detergents. The major
classes of detergent enzymes—proteases, lipases, amylases, and cellulases—each provide specific benefits for application in
laundry and automatic dishwashing. Historically, proteases were first to be used extensively in laundry...
Context in source publication
Context 1
... illustrate the reaction conditions under which en- zymes have to operate, Table 7 shows the components of household detergents in very broad terms. Heavy-duty powdered detergent formulations may vary by geographic regions, with a tendency for higher levels of builder in North America than in Europe and Japan (9). ...
Citations
... For example, for cellulases used in washing powders, mild cellulolytic activity is desirable to avoid bulk degradation of intact cotton fibers. A common cellulase used for this purpose is the GH45 cellulase from Humicola insolens, HiCel45A [10][11][12][13]. ...
Here we describe the first crystal structure of a beta‐1,4‐endoglucanase from a brown‐rot fungus, Gloeophyllum trabeum Gt Cel45A, which belongs to subfamily C of glycoside hydrolase family 45 (GH45). Gt Cel45A is ~ 18 kDa in size and the crystal structure contains 179 amino acids. The structure is refined at 1.30 Å resolution and R free 0.18. The enzyme consists of a single catalytic module folded into a six‐stranded double‐psi beta‐barrel domain surrounded by long loops. Gt Cel45A is very similar in sequence (82% identity) and structure to Pc Cel45A from the white‐rot fungus Phanerochaete chrysosporium . Surprisingly though, initial hydrolysis of barley beta‐glucan was almost twice as fast in Gt Cel45A as compared to Pc Cel45A.
... Microbial proteases are dominant in commercial applications, with a substantial share of the market utilized in laundry detergent [27,195] . They are used as additives in detergent formulations for the removal of proteinaceous stains from clothes, resulting from food, blood, and other body secretions as well as to improve washing performance in domestic laundry and cleaning of contact lenses or dentures [19,196,197] . The use of proteases in detergent products offers colossal advantages since these products contain fewer bleaching agents and phosphates, thus, rendering beneficial effects on public and environmental health [198,199] . ...
Proteases are among the most important classes of hydrolytic enzymes and occupy a key position due to their applicability in both physiological and commercial fields. They are essential constituents of all forms of life, including plants, animals, and microorganisms. However, microorganisms represent an attractive source for protease secretion due to their high productivity in a relatively short time and limited space requirements for cultivation, amongst others. Microbial proteases are produced by submerged or solid-state fermentation process during post-exponential or stationary growth phase. The production of these biocatalysts by microbes is influenced by nutritional and physicochemical parameters. Downstream recovery of high-value enzyme products from culture supernatant using suitable techniques is imperative prior to further use of the biocatalysts. Immobilization of these enzymes in appropriate matrices permits reusability, reclamation, enhanced stability and cost-effectiveness of the biocatalysts. The catalytic properties of microbial proteases help in the discovery of enzymes with high activity and stability, over extreme temperatures and pH for utilization in large-scale bioprocesses. This review provides insights into microbial proteases taking cognizance of the bioprocess parameters influencing microbial proteases production coupled with methods employed for protease purification as well as the immobilization and biochemical properties of the biocatalysts for potential biotechnological applications.
... Alkalophilic organisms have pushed our understanding of life beyond pH 9. The adaptations, survival mechanism, energy production and molecular stability of cellular components have major applications in the field of Industrial applications. Past several years, the successful industrial products has been given by alkalophilic organism including, alkaline amylase (Ozawa et al., 2007), alkaline protease (Fujiwara et al., 1993), alkaline lipases (Chinnathambi, 2015), alkaline celluloses (Kim et al., 2005), alkaline peroxidase (Ikehata et al., 2005), Gaurdzymes (Olsen andFalholt, 1998), Siderophores (McMillan et al., 2010) etc. Despite the several benefits and industrially important features, the non-cultivable organisms would not grow under in vitro conditions. ...
Alkalophiles are a class of extremophiles capable of survival in alkaline (pH roughly 8.5–11) environments, growing optimally around a pH of 10. At such high pH, the normal cellular functions are detrimentally affected for mesophilic organisms. The alkalophiles successfully manage stability of DNA, plasma membrane, and function of cytosolic enzymes, as well as other unfavorable physiological changes at such an elevated pH. A recent development in NextGen sequencing technology facilitates identifying uncultivable organisms amongst the extreme environments. In recent years, distribution of alkalophiles was reported from Soda Lake, marine environments, saline deserts, and natural thermal vents to natural water bodies. Although alkalophiles were first reported in 1889, their enzymatic and industrial applications still make them an interesting area of research. This chapter provides basic information on environmental distribution, taxonomy, physiology, bioenergetics, and survival mechanism and enzymes produced by alkalophilic organisms.
... Enzymes are widely employed in the detergent industry [3], but a key drawback for the use of enzymes in detergent formulations is their stability [4]. The prime ingredients of detergents include surfactants, bleaching agents, builders, foam regulators, corrosion inhibitors, optical brighteners, and other minor additives (e.g., enzymes, perfumes, and fabric tensors) [3][4][5][6]. Surfactants, an essential component in most cleaning products are surface-active compounds that have been extensively applied to a wide range of industrial domains, including detergents, cosmetics, fabric softeners, paints, and emulsions [7]. The molecular interactions between enzymes and surfactants can be beneficial to promoting the catalytic performance [8][9][10][11] and reducing the aggregation propensity [12] of the biocatalysts, or harmful to the enzyme's three-dimensional structure [13]. ...
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.
... The addition of enzymes allows the degradation of dirt and stains. The addition of builders triggers the exchange of calcium ions and magnesium salts, provides alkalinity, and prevents redeposition of impurities [1]. ...
This research aims to determine the characteristics of extra-cellular protease enzymes derived from the intestines of sea cucumbers as a candidate for bio-detergent, to optimize the growth of extra-cellular protease-producing bacteria and to identify the enzymes producing bacteria by DNA sequencing. The study consisted of 5 stages, namely isolation, selection and identification of extra-cellular protease-producing bacterial enzymes, bacterial growth optimization test in the production of extra-cellular protease enzymes, enzyme isolation and characterization, enzyme ability testing of various detergent components and determining the highest conditions of enzyme activity, and purification and identification from the extra-cellular protease enzyme. The results showed that bacteria isolated from the sea cucumbers Stichopus hermanni, Holothuria atra and H.leucopilota. Bacterial isolation derived from the contents of all these sea cucumbers produced 60 isolates and 22 isolates were active against the enzyme protease. Optimization test of carbon compounds (C), namely glucose, fructose, and molasses produces the enzyme molasses. Nitrate (N) compounds optimization test, namely: Ammonium chloride, Ammonium nitrate, Urea found Ammonium nitrate as the best. Optimization test results of the concentration of substances C, N and optimization on the parameters of salinity (25, 30, 35 ppt), pH (6,7,8) and temperature (25, 30, 35 °C), produced the best salinity at 30 ppt, the best ph at 8 and the best temperature at 30 °C. The results of the fermentation test showed that protein hydrolysis in TH.IP.4 isolate media was better than that in THDM.IP.3. There was a positive correlation between cell density and the presence of protease enzymes, where the higher the number of cells, the higher the production of protease enzymes. Protease activity in TH.IP.4 isolates was better than THDM.IP.3 isolates. Molecular identification results showed that isolate 0TH.IP.4 had the closest match (99%) with Bacillus cereus and THDM.IP.3 was a complete match (100%) with Bacillus thuringiensis.
... 4 Furthermore, the combination of protein and surfactants in detergents provides a synergistic effect that enhances the detergency performance compared to that of surfactant-only systems. 5 Other applications where surfactantprotein interactions are of great relevance include sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), for the separation of biological macromolecules, drug delivery, and preservation of formulated food and cosmetic products. 6,7 Due to the fundamental and applied importance of these interactions, researchers have been investigating surfactantprotein systems for almost a century, 8 and still nowadays signicant scientic activity is performed in the eld. ...
The interactions between protein and surfactants play an important role in the stability and performance of formulated products. Due to the high complexity of such interactions, multi-technique approaches are required to study these systems. Here, an integrative approach is used to investigate the various interactions in a model system composed of human growth hormone and sodium dodecyl sulfate. Contrast-variation small-angle neutron scattering was used to obtain information on the structure of the protein, surfactant aggregates and surfactant-protein complexes. 1H and 1H-13C HSQC nuclear magnetic resonance spectroscopy was employed to probe the local structure and dynamics of specific amino acids upon surfactant addition. Through the combination of these advanced methods with fluorescence spectroscopy, circular dichroism and isothermal titration calorimetry, it was possible to identify the interaction mechanisms between the surfactant and the protein in the pre- and post-micellar regimes, and interconnect the results from different techniques. As such, the protein was revealed to evolve from a partially unfolded conformation at low SDS concentration to a molten globule at intermediate concentrations, where the protein conformation and local dynamics of hydrophobic amino acids are partially affected compared to the native state. At higher surfactant concentrations the local structure of the protein appears disrupted, and a decorated micelle structure is observed, we the protein is wrapped around a surfactant assembly. Importantly, this integrative approach allows for the identification of the characteristic fingerprints of complex transitions as seen by each technique, and establishes a methodology for an in-detail study of surfactant-protein systems.
... [2] In the first half of the 20 th century industrial applications of enzymes were limited; the food industry made use of polysaccharide hydrolysing enzymes, [3] while proteases and lipases were utilized in laundry detergent manufacture. [4] The development of molecular biology techniques in the 1970s paved the way for a new era; an era of biotechnology. It is now possible to wield DNA and thus produce proteins in the laboratory. ...
Enzymes have the potential to catalyse complex chemical reactions with unprecedented selectivity, under mild conditions in aqueous media. Accordingly, there is serious interest from the pharmaceutical industry to utilize enzymes as biocatalysts to produce medicines in an environmentally sustainable and economic manner. Prominent advances in the field of biotechnology have transformed this potential into a reality. Using modern protein engineering techniques, in a matter of months it is possible to evolve an enzyme, which fits the demands of a chemical process, or even to catalyse entirely novel chemistry. Consequently, biocatalysis is routinely applied throughout the pharmaceutical industry for a variety of applications, ranging from the manufacture of large volumes of high value blockbuster drugs to expanding the chemical space available for drug discovery.
... The detergents are used in hospitals to clean surgical and endoscopy equipment [39] . These enzymes are used in detergents for laundry and automatic dishwashing to degrade the residues of starchy foods such as potatoes, gravies, custard, chocolate, etc. to dextrins and other smaller oligosaccharides [40,41] ...
The thermostable Alpha-amylase is of greater application. Thermophilic proteins are characterized as high thermal stability proteins. These types of proteins have numerous applications regarding protein engineering, drug design and industrial processes. This review is about the organisms producing Alpha-amylase, family with a maximum number of organisms producing Alpha-amylase, the mechanism of action of the protein, its properties, and the reason for thermostability, the tools used to study the stability of the protein and the industrial applications of Alpha-amylase.
... Cellulases are also used in the laundry and detergent industry which is one of the most popular markets for enzymes sale accounting for 20-30%, with lipase and proteases as major enzymatic components. An innovative approach recently adopted in this industry is the use of alkaline cellulases, protease, and lipase results in a crucial improvement of color brightness and dirt removal from the cotton blend garments (Juturu and Wu 2014b;Olsen and Falholt 1998). ...
The ability of fungi to degrade lignocellulosic materials is due to their highly efficient enzymatic system. Two types of extracellular enzymatic systems were recognized in fungi: they are the hydrolytic system, which produces hydrolases that are responsible for polysaccharide degradation, and a unique oxidative and extracellular ligninolytic system, which degrades lignin and opens phenyl rings. Lignocellulosic residues from wood, grass, agricultural wastes, forestry wastes, and municipal solid wastes are particularly abundant in nature and have a potential for bioconversion. Accumulation of lignocellulosic materials in large quantities in places where agricultural residues present a disposal problem results not only in deterioration of the environment but also in loss of potentially valuable material that can be used in paper manufacture, biomass fuel production, composting, human and animal feed among others. Several novel markets for lignocellulosic residues have been identified recently. The use of fungi in low-cost bioremediation projects might be attractive given their lignocellulose hydrolysis enzyme machinery. This chapter presents a concise account of fungal cellulases as well as their production and key role in bioconversion of lignocellulosic waste. Various aspects of fungal cellulase production using the agriculture wastes and their components have been discussed. Additionally, potential fungal sources of cellulase along with effective bioconversion of agricultural biomass are also summarized.
... Besides SDS, different groups of enzymes, such as proteases, lipases, amylases, and cellulases, are involved in the structure of detergents. 12 Both the anti-lipid and enzymatic capacity accumulated in laundry detergents has motivated researchers to utilize it for the extraction of gDNA. [13][14][15] In a parallel strategy to extract gDNA, the untreated cellulose-based papers have been employed to purify nucleic acids from agarose gel. ...
Here we describe an in-house kit for high throughput DNA extraction using laundry detergent. A simplified lysis buffer made only from 0.08 M EDTA, 0.1 M Tris, and laundry powder is the core of our protocol. We extracted genomic DNA from 150 µL of whole blood collected from different farm animals and compared the performance to both the DNeasy Blood & Tissue Kit (Qiagen) and the widely used salting-out procedure. An evaluation of the concentration and quality of the extracted DNA was then assessed by the NanoDrop absorption spectra, agarose gel migration, amplification in PCR and the Sanger sequencing. The in-house kit successfully extracted clean DNA from all blood samples, and discernably outperformed the commercial kits and the original salting-out procedure in the sense of the simplicity, cost-efficiency, quantity, and the quality of purified DNA. Apart from replacing proteinase K and the sodium dodecyl sulfate treatment by the laundry detergent, our protocol instructs a lysis buffer that eliminates sucrose, Triton X-100, MgCl2, NH4Cl, and KCl. Our handmade kit might be of interest for laboratories in underdeveloped countries with a budget shortage or applications in difficult field conditions, for example, when fridge storage for proteinase K cannot be ensured.
