Overcoming the impediment due to the cost of cellulases production and development of more efficient and specific cellulases are two major goals of future research on cellulases (Sukumaran et al., 2005). The simplest strategy for meeting these goals is to search for novel microbes with high cellulolytic potential. Though it seems that the search for potent cellulolytic microbes in the last few decades has already reached a plateau, but recent studies have shown that many habitats such as extreme environments and relatively unexplored ecosystems still reserve many known as well as unknown cellulase producers, which can exhibit high cellulolytic potency as well as the specificity. The microbes from extreme environments are an attraction …show more content…
A similar approach has been used for obtaining cellulases from anaerobic beer lees converting consortium, wherein the metagenome was sequenced and then screened for cellulase sequences. Thereafter, three cellulase genes, when cloned and expressed in E. coli, were found exhibiting considerable cellulase activities (Yang et al., 2016).
The enhancement in the production of cellulases enzymes is another strategy being attempted consistently for reducing the cost of the cellulases. The use of the low cost renewable substrates can significantly reduce the cost of enzyme production. The lignocellulosic biomass could be used as a raw material for enzyme production (Klein-Marcuschamer et al., 2012; Ellila et al., 2017). The cellulases are inducible enzymes (Acharaya and Chaudhry, 2012). Many of the current commercial cellulases production technologies rely on fungal microorganisms and expression of cell wall degrading enzymes in the filamentous fungi is best induced in the presence of insoluble lignocellulosic substrates (Znameroski et al., 2012; Sohail et al., 2016). Also this has been proposed that enzyme complexes perform best on lignocellulose hydrolysis when the same substrate is used for their production (Sukumaran et al., 2005). The submerged fermentation (SmF) is the most widely used technology for the production of cellulases commercially. However, the problems of longer fermentation times and
There are many differents ways to identify a bacterial unknown and many different situations where identification would be beneficial. One way to identify bacterial unknowns is to perform biochemical tests. In this experiment multiple biochemical tests were done, by performing these tests on the bacterial unknown received the two different bacteria were then identified. The citrate test is done to test the ability of organisms to use citrate as a carbon source. This test uses Simmons citrate agar, the agar contains sodium citrate as the only carbon source and has bromothymol blue as the pH indicator. The organisms that use citrate as a carbon source use the enzyme to transport the citrate into the cell. The cells converts ammonium dihydrogen
40 mL of a concentrated solution of sucrose was prepared at 200mg/mL. Using appropriate dilutions of the stock, 11 solutions including a control solution were made in plastic tubes. The enzyme reaction with sucrose was run in 2 mL volume at room temperature in water. The enzyme constituted half the volume of the stock solution. The substrate was added to the enzyme in order to start the reaction. Each reaction ran for 5 min after which 2 mLs of DNS reagent was added. The solution was boiled for 10 min and the results were read using a spectrophotometer.
Yeast is a fungus that can generate glucose into energy without using any oxygen molecules. We tested the fermenting ability of yeast from two different carbon sources: glucose and aspartame. We hypothesized that yeast is unable to use the carbon sources of aspartame. To do this, we decided to use both carbon sources in the same concentration. Each carbon source was mixed with the same amount of yeast solution. The experiment group of 5.5 mM aspartame solution was compared with the control group of 5.5mM glucose solution. We recorded the rate of fermentation for glucose and aspartame in the Vernier Lab Quest. The fermentation rate of aspartame is a negative number, and glucose is a positive number. Our results show that yeast was unable to ferment aspartame as yeast fermented glucose. The results indicate that aspartame has no effect on yeast fermentation rate because yeast do not catabolize aspartame because it does not have the appropriate enzymes to break it down.
Lactic acid fermentation: Plant and fungal cells produce alcohol as a result of fermentation and animal cells produce lactic acid
Moreover, CtXynGH30 also displayed activity against the polysaccharides having xylan main chain decorated with arabinose side chains such as arabinoxylans. Therefore a range of substrates showing the enzyme activities were treated with CtXynGH30 and the hydrolysed products were analyzed by TLC. The results showed that the enzyme is active against different polysaccharides and produces a series of oligosaccharides. The enzyme is active on xylan main chain polysaccharide substrates like beechwood-, birchwood- and 4-O-methyl glucurono-xylan and capable of releasing oligosaccharides such as xylose, xylobiose and other higher neutral and acidic oligosaccharides (Lane 1-3, Fig. 5). CtXynGH30 also acted over substrates having xylan main chain decorated with various degrees of arabinose side chains like oat spelt xylan, wheat arabinoxylan and rye arabinoxylan and producing xylobiose, xylotriose and other higher oligosaccharides (Lane 4-6, Fig. 5). Furthermore, the TLC profile of CtXynGH30 showed hydrolysis of arabinogalactan and more likely the release of arabino- oligosaccharides (Lane 7, Fig. 5), whereas, arabinan (sugar beet) and xyloglucan did not release any hydrolysed product (Lane 8-9, Fig. 5). The ability of CtXynGH30 to hydrolyse arabinoxylans apart from glucuronoxylans
The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,
The purpose of this lab was to identify two unknown bacteria cultures using various differential tests. The identification of these unknown cultures was accomplished by separating and differentiating possible bacteria based on specific biochemical characteristics. Whether the tests performed identified specific enzymatic reactions or metabolic pathways, each was used in a way to help recognize those specifics and identify the unknown cultures. The differential tests used to identify the unknown cultures were oxidase, catalase, lactose and sucrose fermentation, Kugler/iron agar, nitrate reduction, gelatin hydrolysis, starch hydrolysis, manitol salt, MR-VP, citrate, bile esculin,
Microbial Fuel Cells have a large variety of benefits due to its versatility and choice of fuel.
Amphibacillus xylanus has the capabilities to be both anaerobic and aerobic depending on the environmental setting (Niimura et al. 1990). The EI is an obligate aerobe and grown on a TSA agar plate. Amphibacillus can become aerobic when grown on a TSA plate (Niimura and Suzuki 2015). Both the EI and Amphibacillus xylanus were negative for oxidase and catalase test (Table 4). The indicating factor for this species is its habitat. The EI and A. xylanus were each isolated from the soil (Table 4). This trait sets this species apart from the rest considering the other two species were from aquatic environments. A. xylanus motility indicated a difference from the EI. The EI was shown to have no motility and A. xylanus does have motility. Depending
Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.
Before plating the strains on agar plates, dilutions of the three strains of cells were prepared with LB broth.
2. Introduction: Each student was given unknown bacteria and was instructed to perform a variety of experimental tests that would help to identify their bacteria. During the process of identification, the unknown bacteria was added to many different testing medias using aseptic technique. They are as follows: lactose fermentation on eosin methylene blue (EMB), TSI (Triple Sugar Iron agar), Phenol red sucrose, the SIM test, H2S by SIM, IMViC (indole, motility, voges-proskauer, and citrate), Urease (urea broth), PDase (Phenylalanine Deaminase), Lysine Decarboxylase, and Ornithine Decarboxylase. Colonial morphology on EMB was used to
Introduction: Through the conduction of numerous experiments, the identity of two bacterial isolates was determined. The tested specimen was an unknown sample of a mixed culture of two different species of bacteria. The first step that was taken was obtaining a pure culture of each species of bacteria by isolating one species from the other. Once isolation was complete, the isolated cultures were tested using procedures that had been performed during previous lab sessions. A gram stain was performed on the two isolates. The isolate which had tested gram negative was then tested for the presence of cytochrome C and lactose fermentation. For the gram positive isolate, cell shape was determined and a catalase test was performed.
In industrial scale production, microorganism such as bacteria and fungi was fully expressed the lipase. The advantage of using bacteria producing
Agro-industrial wastes are at most composed of complex polysaccharides that might serve as nutrients for microbial growth and production of enzymes, several microorganisms are capable of using