@article{fdi:010065248,
  title = {{P}artial purification and characterization of alpha-amylases from {A}brus precatorius, {B}urnatia enneandra and {C}adaba farinosa},
  author = {{K}lang, {M}.{J}. and {T}alamond, {P}ascale and {D}jidimbele, {N}. and {T}avea, {F}. and {N}djouenkeu, {R}.},
  editor = {},
  language = {{ENG}},
  abstract = {{L}eaves of {A}brus precatorius, tubers of {B}urnatia enneandra and stems of {C}adaba farinosa are used in savannah regions of {C}ameroon in traditional food processing, particularly in sweetening and liquefaction of gruels. α-amylase was extracted and partially purified from these plants using conventional methods of protein purification including ammonium sulfate fractionation and two steps of gel filtration. {P}urification achieved 58, 61 and 46 fold respectively for {A}. precatorius, {B}. enneandra and {C}. farinosa. {T}he purified enzymes were then characterized in terms of molecular weight, optimum p{H} and stability, optimum temperature and stability, {K}m, {V}max and metals ions effects. {T}he optimum p{H} of enzymes varied from 6.0 for amylases from {B}. enneandra and {C}. farinosa, to 7.0 for amylase from {A}. precatorius; while the optimum temperature was 60°{C} for amylases from {A}. precatorius and {B}. enneandra, and 65°c for amylase from {C}. farinosa. {T}he three enzymes displayed, respectively for {A}. precatorius, {B} enneandra and {C} farinosa, a molecular weight of 60, 65 and 48.5 k{D}a, {K}m for hydrolyzing soluble starch of 3.25, 1.81 and 3.18 mg/ml, and strong individual activation by {C}a2+, {C}o2+ and {F}e3+. {L}i2+ appeared as a common activator for all the amylases, while {A}g+, {H}g2 +, {Z}n2+ and {C}u2+ act as common inhibitors.},
  keywords = {{CAMEROUN}},
  booktitle = {},
  journal = {{J}ournal of {E}nzyme {R}esearch},
  volume = {5},
  numero = {1},
  pages = {66--71 [art. {BIA}0002353]},
  ISSN = {0976-7657 ; 0976-7665},
  year = {2014},
  URL = {https://www.documentation.ird.fr/hor/fdi:010065248},
}