Water vapor adsorption and desorption isotherms of biologically active proteins.
Using a protein isolated from soy, a dynamic water adsorption method was developed and the data were compared with those obtained from a static gravimetric procedure. Both methods gave comparable results, showing that Type II isotherms with considerable hysteresis were obtained. However, the dynamic procedure was preferred since it provided data rapidly and used significantly less material. Using the dynamic method, water adsorption isotherms at 25 degrees C were also determined for four biologically active proteins: alpha-amylase, beta-glucuronidase, lipase, and urease. BET (Brunauer, Emmet, and Teller) parameters were calculated and the specific surface areas for the native, biologically active proteins were found to be similar, 238.4 +/- 20.2 m2/g. On the other hand, the specific surface area for the denatured soy protein isolate was 144.6 m2/g. Nevertheless, the heat of absorbance for all of the proteins examined was similar, suggesting that they have comparable degrees of hydrophilicity.
Teng
C D
CD
Pharmaceutics Department, College of Pharmacy, University of Illinois, Chicago 60612.
Zarrintan
M H
MH
Groves
M J
MJ
D000327:Adsorption; D005966:Glucuronidase / Q000737:chemistry; D006813:Humidity; D008049:Lipase / Q000737:chemistry; D014674:Plant Proteins, Dietary / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D030262:Soybean Proteins; D014835:Volatilization; D014867:Water; D000516:alpha-Amylases / Q000737:chemistry
D014674:Plant Proteins, Dietary; D011506:Proteins; D030262:Soybean Proteins; D014867:Water; D008049:Lipase; D000516:alpha-Amylases; D005966:Glucuronidase