Lipases are enzymes that break down the fats. Esters formed from glycerol and fatty acids are catalyzed and hydrolyzed by these enzymes. They are used in many biotechnological processes and have applications in food, cosmetics, detergents, pharmaceutical industries and industrial waste management. Numerous efforts have been done to isolate lipase producing microbes. Microbial lipases are commercially important, microbes like bacteria, yeast and fungi produce lipases. These microbes are found in diverse environment such as industrial wastes, vegetable oil processing factories, oil mill effluent and soil contaminated with oil. We can isolate these micro-organisms from above mentioned habitats and can increase their lipase producing activity by These enzymes are widely used in numerous biotechnological processes and have applications in cosmetic, detergent, food, pharmaceutical industries and leather (Rajeshkumar, Mahendran et al. 2013). Lipases form an essential part of the industries range from dairy, agrochemical and detergents to oleo-chemicals, tea industries, and in numerous bioremediation processes. The potential for marketable utilization of a microbial lipase is firm by its yield, stability, activity, and other distinctiveness (Shu, Jiang et al. 2010). Because of the huge applications, newer microbes are to be screen for production of lipases having wanted properties. The considerate of the study will facilitate us to tailor new lipases for biotechnological applications (Verma, Thakur et al.). Thus lipases are credible tools for the organic chemists. The widen applications of microbial lipases in biotechnology has necessitate the continued research and development of novel lipases with large substrate tolerance, and high stability (Momsia and Momsia 2010). Lipases of microbial origin are extensively diversify in their enzymatic properties and substrate specificity, which make them most attractive for industrial applications. (Hasan, Shah et al. 2013). Some important lipase-producing bacterial genera are Bacillus, Pseudomonas and Burkholderia and fungal genera include Aspergillus, Penicillium, Rhizopus, Candida. Different species of yeasts belonging to seven different genera include Zygosaccharomyces, Pichia, Lachancea, Kluyveromyces, Saccharomyces, Candida, and Torulaspora. (Verma, Thakur et al.). Lipases are classified into serine hydrolases and they catalyze both the hydrolysis and synthesis of long-chain triacylglycerols. Extracellular lipases are created by microorganisms, fungi and bacteria. Lipases from bacteria have been salaried much consideration due to their frequent usage in a range of biotechnological applications. Pseudomonas lipases are the most central ones which have a important potential in detergent industry and organic chemistry (Aysun 2009). Bacterial strain are usually more used as source of lipases because they present higher activities compared to yeast. Fungal lipases which are report to be derivative mainly from Candida and Aspergillus sp and Geotrichum sp. are mainly significant in industrial applications (Nwuche and Ogbonna 2011). The bacterial strain Bacillus sp. strain DVL2 has been shown
Casullo De Ara 'Ujo, H. W., Fukushima, K. and Takaki, G. M. C. 2010. Prodigiosin production by Serratia marcescens UCP 1549 using renewable-resources as a low cost substrate. Molecules, 15 (10), p. 6931-6940.
The eighteenth exercise of the laboratory manual titled Unknown Identification and Bergey’s Manual is an experiment to identify an unknown bacterium. In this exercise, a student must randomly choose a numbered bacterium available to the class. The keys in Appendix H, located on the last pages of the book, are the major helpful tools in this exercise because it provides completed steps of tests that needs to be performed in order to distinguish certain bacteria. This means that in this exercise, various types of tests and techniques must be performed to identify the chosen unknown bacterium. The unknown bacterium that I selected was number thirty-nine in which I discovered as the Bacillus megaterium after conducting several tests.
The Effect of Temperature on an Enzyme's Ability to Break Down Fat Aim: To investigate the effect of temperature on an enzyme’s (lipase) ability to break down fat. Hypothesis: The graph below shows the rate increasing as the enzymes get closer to their optimum temperature (around 35 degrees Celsius) from room temperature. The enzyme particles are moving quicker because the temperature increases so more collisions and reactions occur between the enzymes and the substrate molecules. After this the graph shows the rate decreasing as the enzymes are past their optimum temperature (higher than). They are getting exposed to temperatures that are too hot and so the proteins are being destroyed.
Bacillus globigii. (n.d.) WordNet 3.0, Farlex clipart collection. (2003-2008). Retrieved March 20 2014 from http://www.thefreedictionary.com/Bacillus+globigii
An Investigation into the Effect of Lipase Concentration on the Hydrolysis Of Fats Using the data loggers a recording of the pH was taken every 5 seconds and for each experiment the data loggers produced graphs of the change in pH. From each of these graphs a gradient was calculated which showed the rate of pH change per second. Firstly I calculated the gradients by choosing the steepest section of the graph and dividing the change in pH of this section by the time. However this method proved to be quite inaccurate giving very varied results, for example in these results the average rate of reaction for the 4% lipase solution (-0.457 pH/min) was lower than the 3% lipase solution (-0.471 pH/min). Also the rates in the 2% lipase solution ranged from -0.01 pH/min to -0.95 pH/min showing little reliability in the results. This was partly as I was only guessing which the steepest part of the graph was.
The objective of this lab was to identify unknown bacteria culture by using various differential tests. There are many reasons for knowing the identity of microorganisms including to find the correct antibiotic to treat infections the bacteria may have caused. All the methods and techniques used to identify unknown bacterium #79 was learned in the microbiology laboratory.
...he viability of the microorganism nor the biological potency of the LPS. Deoxysugars are frequent components in O-chain structures but sugars that are more characteristic of the inner core region like heptose are seldom present. The most common substituents are O- and N- acetyl phosphate and phosphorylethanolamine groups. Amino acids in amide linkages, acetamidino groups as well as formyl groups and glyceric acid are often found as non stoichiometric substituents(Brade et al., 1999). The extended O-polysaccharide chains out from the bacterial outer membrane acts as a shield which enable the bacteria to get away from the lytic activity provided by the complement cascade. Many gram negative strains require O-polysaccharide as an essential component for the survival in host system as it prevents the attack from complement membrane attack complex (Joiner et al., 1984).
...osphorus and other essential trace elements in non-ruminants feed (Lan et al., 2011). Nevertheless, the Mitsuokella jalaludinii is an anaerobic bacterium and therefore need rigid growth conditions for it to be mass produced. One of the possible solutions for this problem is to clone and express the phytase genes into other microorganisms which are aerobe or facultative anaerobe in nature without compromising its existing phytase activity. The whole genome of Mitsuokella jalaludinii has been sequenced and the genes responsible for the expression of phytase, Phy1 and Phy2, were identified through the gene annotation of the genome and are in close proximity to each other. As such, the need for cloning and further expression of the Mitsuokella jalaludinii phytase is essential to identify the potential of this enzyme to be largely produce for commercialization purposes.
Nuclease is one of the acknowledged proteins secreted by members of the genus Lactobacillus. After several evidences of extracellular DNAse activity, nucleases from several Lactobacillus species have been identified by two methods; sodium dodecyl sulfate polyacrylamide gel electrophoresis, coupled to in-gel protein renaturalization and nuclease assay [28]. It has been shown that nuclease activity over the DNA present in the luminal content, can lead to the formation of a set of diverse oligonucleotides, some of them with immunomodulatory properties [29, 30, 31].
The enzymes have active sites on their surfaces to allow the binding of a substrate through the help of coenzymes to form enzyme-substrate complex. The chemical reaction thus converts the substrate to a new product then released and the catalytic cycle proceeds.
According to the gram-positive table, the unknown gram-positive microbe is Bacillus subtilis (4). Comparing these results with known biochemical characteristics of B. subtilis, all results are consistent except for the lactose test. B. subtilis is not a lactose fermenter (5). This error could be due to contamination or incorrect incubation time.
They are produced by an extensive variety of microorganisms including microscopic organisms, molds, and yeasts further more mammalian tissues. The vast majority of the commercial alkaline proteases were separated from Bacillus species (Maurer, 2004). An impressive number of fungal species are known to produce extracellular basic proteases, for example, Conidioboluscoronatus (Phadatare et al., 1993), Arthrobotrysolgospora (Tunlid et al.,1994), Trichodermaharzianum (Dunaevsky et al., 2000), Cephalosporium sp. KM388 (Tsuchiya et al.,1987) and Aspergillus Fumigatus (Wang et al.,2005). Alkaline proteases of microbial origins have significant mechanical potential because of their biochemical differences and wide applications in tannery and food industries, medicinal formulations, cleansers and procedures like waste treatment, silver recuperation and determination of amino corrosive blends (Rao et al., 1998; Agarwal et al., 2004). The alkaline proteases locate their biggest use in house hold clothing with an overall yearly production of cleansers of more or less 13 billion tons (Nehra et al.,
Enzymes, such as cellulases, which catalyse the breakdown of cellulose, have been isolated from several different organisms, including fungi. However, the purification of enzyme from these sources is expensive, on the order of $5.50 per gallon of ethanol produced. Genetic engineering or biotechnology has already played a key enabling role in the development of cellulosic biomass conversion technologies by dramatically reducing the cost of cellulase production from about $5.50 per gallon of ethanol to $0.10-15 per gallon of
Immobilization of enzyme on hydrogel involves sequence of steps which is shown in Figure 12. They are (i) activated agarose discs (Agar–OH) with glycidol (2, 3-epoxypropanol) to form an intermediate glyceryl-agarose (Agar–O–CH2–CHOH– CH2OH); (ii) oxidized glyceryl agarose with periodate to produce glyoxyl-agarose (Agar–CH2CHO); (iii) enzyme coupling to the aldehyde groups via the Schiff base reaction; (iv) reduction with sodium borohydride produces an enzyme-agarose
The economies of most developing countries dictates that materials and resources must be used to their full potential, and this has propagated a culture of reuse, repair and recycling. Municipal solid waste is composed of 40-50% cellulose, 9-12% hemicellulose and 10-15% lignin on a dry weight basis. Recently, cellulose has been in the public eye due to its possible use in the production of useful products. It is the most abundant biological organic compound on earth. It is a linear glucopolymer compound of anhydro-glucose units joined to each other by β-1,4-glucosidic bonds. Microorganism performs their metabolic processes rapidly and with remarkable specificity under ambient conditions, catalyzed by their diverse enzyme mediated reactions. An enzyme alternative to harsh chemical technologies has led to intensively exploration of natural microbial biodiversity to discover enzymes.