The dialysed enzyme was loaded onto a column of Sephadex G-50 (120 cm × 1.0 cm) equilibrated with 10 mM Tris-HCl buffer‚ pH 8. The column was eluted at a flow rate of 1 ml / 6 min. The elution profile of gel filtration chromatography is shown in the (Fig: 1). The fractions collected were determined for its total protein concentration and fibrinolytic enzyme activity. The active fraction obtained was pooled together‚ concentrated by lyophilization and used as purified fibrinolytic enzyme for subsequent
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importance to industry and sparked a large interest into the exploration of enzyme activity in microorganisms. Amylase is one of the most widely used enzyme required for the preparation of fermented foods. Apart from food and starch industries‚ in which demand for them is increasing continuously‚ amylase is also used in various other industries such as paper and pulp‚ textiles‚ and medical labs. The global market for enzymes was about $2 billion in 2004 (Sivaramakrishnan et al.‚ 2006). Fungi belonging
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EXPERIMENT 13 DIGESTION IN THE SMALL INTESTINES ------------------------------------------------- ABSTRACT The small intestine serves as the site of major digestive and absorptive processes. In this experiment‚ the action of pancreatic enzymes on representative samples of each food group under different conditions‚ such as increased/decreased pH and presence of other substances‚ were observed. A pancreatin solution was first prepared from a hog pancreas and was completely neutralized using
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Abstract Enzymes are biological catalysts that speed up the rate of chemical reactions by lowering the reactants’ activation energy. The goal of this lab was conducted to determine the optimal temperature for bacterial and fungal Amylases and evaluate how temperature affects the catabolic rate of enzymes. Enzyme reaction rate was measured using an Iodine test in which drops of starch solution with either fungal or bacterial Amylase exposed to different temperatures were mixed with Iodine. Iodine
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Interactions BigIdea 4 investigation 13 ENZYME ACTIVITY* How do abiotic or biotic factors influence the rates of enzymatic reactions? ■■BACKGROUND Enzymes speed up chemical reactions by lowering activation energy (that is‚ the energy needed for a reaction to begin). In every chemical reaction‚ the starting materials (the substrate(s) in the case of enzymes) can take many different paths to forming products. For each path‚ there is an intermediate or transitional product between reactants and
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INVERTASE FROM YEAST AND EFFECT OF pH ON ENZYMATIC ACTIVITY Jenelle C. Faustino‚ John Gambit B. Garcia‚ Fatima S. Jusay‚ Oliver Alexander B. Lao and Eunice L. Licudine Group 4 2 E Medical Technology Biochemistry Laboratory ABSTRACT Enzymes are substances that are produced by living organisms and act as catalysts in order to speed up or chance a chemical reaction without changing itself at the end of the reaction. Invertase was extracted first from baker’s yeast. Determination of the
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ABSTRACT Enzymes are highly specific and can distinguish isomers of the same molecule. The enzyme invertase specifically catalyzes the reaction of the conversion of sucrose to its individual carbohydrates glucose and fructose. It does not catalyse the reaction of maltose to 2 glucose or lactose to galactose. In this experiment‚ titrimetric and spectrophotometric methods were used to determine the specificity of invertase by determining the amount of glucose converted from the given disaccharides
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CYTOCHROME P450 2S1 Cytochrome P450s (CYPs) are monooxygenase proteins that catalyze the metabolism of exogenous and endogenous substrates. CYPs function as enzymes and are found in all kingdoms of life. The P in P450 refers to pigment and 450nm refers to the wavelength of CYPs in solution exposed to carbon monoxide (CO). CYPs belong to the superfamily of proteins containing a heme (iron) cofactor active site. The heme active site is tethered to the CYP protein via thiolate ligand derived from
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Introduction Hydrolysis is a chemical reaction that uses water to split complex molecules. The water molecule H2O is split in the mechanism of hydrolysis‚ hydrogen cations and hydroxide anions. When the enzyme catalyzes its reaction inside the cell‚ it is referred to as intracellular hydrolases. When the enzymes secreted from the organism to catalyze reactions outside the cell‚ it is referred to as exoenzymes or extracellular hydrolases. Four hydrolysis reactions are discussed in the report‚ bile esculin
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certain temperature‚ the enzymes will become denatured and then the rate will decrease. Each enzyme functions at an optimum pH. Well according to the graph‚ you see that the enzyme did not function at all when boiled which can be explained by the fact that it got denatured. Denaturing means the secondary and tertiary structure of the enzyme does get disrupted so bonds would definitely be broken. What seemed to be the optimum temperature and pH for the enzyme? In other words‚ at what temperature
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