Folia Microbiologica

, Volume 11, Issue 6, pp 422–438 | Cite as

Amylolytic enzymes ofEndomycopsis capsularis

II. A study of the properties of isolated α-amylase, amyloglucosidase and maltase-transglucosidase
  • Helena Ebertová


Crude enzymatic preparations were prepared from supernatants of submerged cultures ofEndomycopsis capsularis 311/1. Fractions exhibiting amyloglucosidase, α-amylase and maltase-transglucosidase activities were isolated using chromatography on DEAE cellulose. Separation by paper electrophoresis shows that α-amylase moves most rapidly to anode, amyloglucosidase is slower and maltase-transglucosidase is very slow. α-Amylase has a pH optimum of activity about 4.5, stability optimum lies within the range of 4.8–7.0 at 20°C. Temperature optimum lies between 40 and 50°C, activation energy is 8,150 cal between 20 and 45°C. The enzyme forms a mixture of erythrodextrins and oligosaccharides of a maltose series from amylose and β-limitdextrin. It degrades more slowly maltotetraose and maltose, oligosaccharides of isomaltose series are not degraded. Amyloglucosidase has the same pH optimum of activity at 4.5 and is stable within the range of pH 4.2–8.0 at 20°C. Temperature optimum is between 40–50°C, activation energy is 7200 cal between 20–45°C. It forms glucose from amylose, β-limitdextrin, maltotetrose, maltose, isomaltotetrose and isomaltose. The reaction rate decreases with decreasing molecular weight, linear substrates with α(1→6) glucosidic bonds are hydrolysed 50-times slower than compounds containing α(1→4) glucosidic bonds and having the same length of glucosidic chain. Maltase-transglucosidase has pH optimum of activity about 4.6. It is stable within the range of pH 5.5–6.8. Temperature optimum for the formation of glucose and transglucosidase products is about 40°C, activation energy is 10,900 cal between 20–40°C. Reaction rate decreases with increasing length of the molecule of substrate. It decreases much more slowly with substrates of the maltose series than with those of the isomaltose series. Michaelis constant Km is 2.94×10−3 m for maltose and 2.13×10−2 m for isomaltose. The enzyme activity is not influenced by iodoacetate, ferricyanide, HgCl2, ethylenediamine-tetraacetic acid and NaF. The enzyme is inhibited by γ- and δ-gluconolactone at concentrations of 0.5 mmole and higher; “uncompetitive” inhibition is apparently involved, Ki=0.235. A relative occurrence of reaction products is not influenced by the length of chain of substrates of the maltose series. It is also not influenced by the concentration of substrates during initial steps of the reaction. A relative amount of transglucosidation products increases with increasing concentration of substrates during late phases of the reaction.


Amylase Maltose Amylose DEAE Cellulose Maltotriose 
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Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 1966

Authors and Affiliations

  • Helena Ebertová
    • 1
  1. 1.Department of Technical Microbiology, Institute of MicrobiologyCzechoslovak Academy of SciencesPrague 4

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