How can you tell amylase is an exoenzyme and not an endoenzyme?
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Exoenzymes work outside of cells.  Endoenzymes work inside of cells.\n\nIn humans, amylase is present in the saliva as wells as the small intestine (secreted from pancreas).  Since the enzyme works to break down ingested carbohydrates from food as it passes through the gastrointestinal tract, an extracellular space, it is an exoenzyme.
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Benedict's Test only tests positive for simple reducing sugars.  Starch is a polysaccharide.
878920
"why betaD glucose stabler than alphaD glucose in aquas solution?"\n\nbeta conformation is more stable cuz more branching -OH groups are in equatorial positions than alaph conformation.\n\n"why mutarotation proceeds slowly in heavy water?"\n\nmutarotation need to open the ring first [same reason with why it dosen't mutarotate in pyridine or in phenol alone]\n\n"how to differentiate between erythrose & threose using reduction reaction?"\nreduce both erythrose and threose to alcohol. erythrose is optically inactive, threose is active.\n\n"which D-aldohexoses produce meso-aldaric acid when react with HNO3 ?"\nD- allose and D- galactose\n\n"why do not methylglycosides do not react with fehling's solution & tollen's reagent and do not mutarotate?"\n\nbecause you cant open methylglycosides chain to form the straight chain aldose back. Only aldehyde can react with tollen's agent.
89534
Salivary amylase catalyses the breakdown of starch (and glycogen) into maltose.\nThe process of digestion in the mouth is only brief because the masticated food is soon swallowed into the stomach.\nThe hydrochloric acid in the stomach stops any further digestion of starch.\nOnce the stomach contents enter the small intestine, pancreatic juices both neutralise the stomach acid and supply more enzyme - pancreatic amylase.\nSo the digestion of starch (and glycogen) is completed in the small intestine.
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figure out the efgfect of the enzyme. Or you can test DNA structure. Inhibitary enzymes have a blacked actionsite whereas activation enzymes have activation sites open to substrates
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The empirical formula of glycogen is(C6H10O5)n.\n                                       \nGlycogen is a highly-branched polymer of 10,000 to 120,000 Glc residues and molecular weight between 106 and 107 daltons. Most of Glc units are linked by a α-1,4 glycosidic bonds, approximately 1 in 12 Glc residues also makes a α-1,6 glycosidic bond with a second Glc which results in creating of a branch. Glycogen has only one reducing end and a large number of nonreducing ends with a free hydroxy group at carbon 4. The glycogen granules contain both glycogen and the enzymes of glycogen synthesis (glycogenesis) and degradation (glycogenolysis). The enzymes are nested between the outer branches of the glycogen molecules and act on the nonreducing ends. Therefore, the many nonreducing end-branches of glycogen facilitate its rapid synthesis and breakdown.
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Pancreatic juice contains three digestive enzymes: tryptase, amylase, and lipase, that, along with intestinal enzymes, complete the digestion of proteins, carbohydrates, and fats, respectively.
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Everyone who answered already are blithering idiots. All fungi produce exoenzymes that break down the substrate (food) that their spores land on. Similar to flies, fungi produce these enzymes to break down foods into simple sugars that they can then easily absorb. Different fungi produce different exoenzymes. Therefore, if a fungal spore happens upon a particular substrate (food) for which it doesn't produce the proper exoenzyme, it will not grow on that food. The best substrates are potato extract agar and malt extract agar.
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A monosacharide is one that has not condensed with other sugars to make a disaccharide or a polysaccharide.  If you polymerize glucose, you get glycogen, which is created by the condensation of many glucose molecules together.  Starch and fiber etc. are polymers (polysaccharides, meaning "many sugars") containing many linked subunits, and the subunits are each called monosaccharides (literally, "one sugar").
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when you get a pancreatitis (inflammation of the pancreas), the pancreatic secretion may enter the pleural space through retroperitoneal space. so if amylase raises in pleural fluid, it may indicates that effusion is of pancreatic origin. \nglucose helps differentiate the nature of pleural fluid.\nfor example, glucose > 40 mg/dl: no infection\nglucose < 40mg/dl: infection probable.
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water is smallest, then glucose , then starch is bigger.\n\nI do not know what IKI is , nor how big it's molecule is, so Ido not know where to slot it in.
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2. The temperature that was the most favorite condition for amylase_catalyzed hydrolysis was cold, I tested it at 1.7°C.
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Well I don't know much about it but look at it this way: what happens normally when starch reacts with amylase? I'm guessing that sugar is produced. If so, I would be willing to bet that when you increase the amount of starch, the rate that sugar is produced increases (enzyme makes contact with starch molecules more frequently, as there is more of it to hit). Of course this will only happen up to a point. Once a certain amount has been added, the amylase will be at its maxium speed of sugar converting, so the speed will stay the same.\n\nI hope this helps, good luck!
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Amylase - occurs in the human mouth, breaking down starch, which is impossible for humans to digest.\n\nLipase - acts of lipids (fatty acids), breaking them down into simpler , more easily degradable substances.\n\nMaltose - acts on poly proteins to transfrom them into simpler amino acids
909484
In addition to what Jen said, I would also like to point out that although isoenzymes by definition catalyze the same reaction, they often do it with different kinetic parameters.\n\nFor example, there may be different reaction order, affinities (K-constants), and the like, between two isozenzymes, even though they both perform the same product-to-substrate conversion.
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This is not a pure biology question. Should be bio-chemistry.
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(m)\n\nmetabolic pathway analysis, it should be considered that many enzymes operate with low specificity (e.g. nucleoside diphosphokinase, uridine kinase, transketolase, aldolase), so that various substrates and products can be converted. Here, we analyze the effect of enzymes with low substrate specificity on the elementary flux modes (pathways). We also study the benefits of two different approaches to describing multifunctional enzymes. The usual description is in terms of (overall) enzymatic reactions. At a more detailed level, the reaction steps (half-reactions, hemi-reactions) of the formation and conversion of enzyme-substrate complexes are considered. Multifunctional enzymes operate according to various mechanisms. This is illustrated here by the reaction schemes for the different enzyme mechanisms of bifunctional enzymes. For enzymes with two or more functions, it is important to consider only linearly independent functions, because otherwise cyclic elementary modes would occur which do not perform any net transformation. However, the choice of linearly independent functions is not a priori unique. We give a method for making this choice unique by considering the extreme pathways of the hemi-reactions system. A formal application of the algorithm for computing elementary flux modes (pathways) yields the result that the number of such modes sometimes depend on the level of description if some reactions are reversible and the products of the multifunctional enzymes are external metabolites or some multifunctional enzymes partly share the same metabolites. However, this problem can be solved by appropriate interpretation of the definition of elementary modes and the correct choice of independent functions of multifunctional enzymes. The analysis is illustrated by a biochemical example taken from nucleotide metabolism, comparing the two ways of description for nucleoside diphosphokinase and adenylate kinase, and by several smaller examples.