Sie befinden Sich nicht im Netzwerk der Universität Paderborn. Der Zugriff auf elektronische Ressourcen ist gegebenenfalls nur via VPN oder Shibboleth (DFN-AAI) möglich. mehr Informationen...
Physicochemical and Enzymatic Properties of Benzyl Isothiocyanate Derivatized Proteinases
Ist Teil von
Journal of agricultural and food chemistry, 1998-12, Vol.46 (12), p.5043-5051
Ort / Verlag
Washington, DC: American Chemical Society
Erscheinungsjahr
1998
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
This paper deals with interactions of benzyl isothiocyanate (benzyl-ITC) with cysteine proteases (bromelain and papain) as well as with serine proteases (trypsin and α-chymotrypsin). The derivatives formed with different amounts of benzyl-ITC (10−125 mg of benzyl-ITC/g of protein) have been characterized in terms of their physicochemical and proteolytic properties. Detectable changes in the chromatogram pattern of the derivatives coupled with an increase in hydrophobicity were documented by RP-HPLC. Furthermore, the isoelectric point was shifted to the lower pH values. SDS−PAGE and MALDI-MS of the chymotrypsin derivatives showed distinctive molecular changes. The other major subject of the present paper shows the effects of benzyl-ITC derivatization on proteolytic activity of bromelain, papain, trypsin, and α-chymotrypsin. In general, a decrease of enzyme activity was documented for the proteolysis of casein and myoglobin as substrates. Keywords: Isothiocyanates; enzyme derivatization; bromelain; papain; trypsin; α-chymotrypsin; proteolytic degradation; casein; myoglobin; RP-HPLC; IEF; MALDI-MS