Parigi Ramesh Kumar
Central Food Technological Research Institute
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Featured researches published by Parigi Ramesh Kumar.
Journal of Agricultural and Food Chemistry | 2008
Kamsagara Basavarajappa Devaraj; Parigi Ramesh Kumar; Vishweshwaraiah Prakash
Ficin (EC 3.4.22.3), a cysteine proteinase isolated from the latex of a Ficus tree, is known to occur in multiple forms. Although crude ficin is of considerable commercial importance, ficin as such has not been fully characterized. A major ficin from the commercial crude proteinase mixture preparation of Ficus carica was purified and characterized. The purified enzyme was homogeneous in both sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and gel-filtration chromatography and is a single polypeptide chain protein with a molecular mass of 23 100 +/- 300 Da as determined by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF). The enzyme was active in the pH range of 6.5-8.5, and maximum activity was observed at pH 7.0. The N-terminal core sequence of ficin has homology with N-terminal sequences of plant cysteine proteinases. The enzyme contains three disulfide bonds and a single free cysteine residue at the active site. The effect of co-solvents, such as sorbitol, trehalose, sucrose, and xylitol, on the thermal stability of ficin was determined by activity measurements, fluorescence, and thermal denaturation studies. The apparent thermal denaturation temperature (T(m)) of ficin was significantly increased from the control value of 72 +/- 1 degrees C in the presence of all co-solvents. However, the maximum stabilization effect was observed in terms of thermal stabilization by the co-solvent trehalose.
International Journal of Biological Macromolecules | 2009
K.B. Devaraj; Parigi Ramesh Kumar; V. Prakash
Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about approximately 74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography.
Food Chemistry | 2008
C. Radha; Parigi Ramesh Kumar; V. Prakash
Journal of Food Science | 2007
M.P. Raghavendra; Parigi Ramesh Kumar; V. Prakash
International Journal of Biological Macromolecules | 2007
H.A. Sathish; Parigi Ramesh Kumar; V. Prakash
Journal of the Science of Food and Agriculture | 2008
C. Radha; Parigi Ramesh Kumar; Vishweshwaraiah Prakash
Process Biochemistry | 2009
Sijo Mathew; B.A. Shamasundar; Parigi Ramesh Kumar; V. Prakash
Process Biochemistry | 2009
Hasige A. Sathish; Parigi Ramesh Kumar; Vishweshwaraiah Prakash
European Food Research and Technology | 2010
Gangadhara; Parigi Ramesh Kumar; V. Prakash
European Food Research and Technology | 2008
M.P. Raghavendra; Parigi Ramesh Kumar; Vishweshwaraiah Prakash