Kaur Tajwinder, Kaur Amandeep, Grewal Ravneet K
Department of Biochemistry, School of Biotechnology and Biosciences, Lovely Professional University, 144401 Phagwara, Punjab India.
J Food Sci Technol. 2015 Sep;52(9):5954-60. doi: 10.1007/s13197-014-1639-5. Epub 2014 Nov 14.
The kinetics of cysteine and divalent ion modulation viz. Ca(2+), Cu(2+), Hg(2+) of fruit bromelain (EC 3.4.22.33) have been investigated in the present study. Kinetic studies revealed that at pH 4.5, cysteine induced V-type activation of bromelain catalyzed gelatin hydrolysis. At pH 3.5, Ca(2+) inhibited the enzyme noncompetitively, whereas, both K-and V-type activations of bromelain were observed in the presence of 0.5 mM Ca(2+) at pH 4.5 and 7.5. Bromelain was inhibited competitively at 0.6 mM Cu(2+) ions at pH 3.5, which changed to an uncompetitive inhibition at pH 4.5 and 7.5. An un-competitive inhibition of bromelain catalyzed gelatin hydrolysis was observed in the presence of 0.6 mM Hg(2+) at pH 3.5 and 4.5. These findings suggest that divalent ions modulation of fruit bromelain is pH dependent.
本研究考察了半胱氨酸和二价离子(即Ca(2+)、Cu(2+)、Hg(2+))对菠萝蛋白酶(EC 3.4.22.33)的调节动力学。动力学研究表明,在pH 4.5时,半胱氨酸诱导菠萝蛋白酶催化明胶水解的V型激活。在pH 3.5时,Ca(2+)非竞争性抑制该酶,而在pH 4.5和7.5时,在0.5 mM Ca(2+)存在下观察到菠萝蛋白酶的K型和V型激活。在pH 3.5时,0.6 mM Cu(2+)离子竞争性抑制菠萝蛋白酶,在pH 4.5和7.5时则变为非竞争性抑制。在pH 3.5和4.5时,在0.6 mM Hg(2+)存在下观察到菠萝蛋白酶催化明胶水解的非竞争性抑制。这些发现表明,二价离子对菠萝蛋白酶的调节是pH依赖性的。