Articles
PROTEOLYTIC ACTIVITY OF GARLIC CALLI (ALLIUM SATIVUM, L.)
Article number
501_28
Pages
185 – 190
Language
Abstract
Tissue culture of garlic (Allium sativum, L.) was evaluated for proteolytic activity.
Biochemical parameters, such as optimum pH, optimum temperature range, thermal stability and protein content of the enzyme preparation were assessed.
Acetonic powder of the calli was prepared with acetone at – 20°C in a 25% w/v rate.
Extractives obtained by gentle stirring with phosphate buffer pH: 7.0 containing 5 mM EDTA (protein content 0.45 g per 100 g of acetonic powder) showed good thermal stability at moderate temperatures and higher proteolytic activity (tested with azocasein, azocoll and haemoglobin as substrates) at pH: 5.0–6.0. The use of a variety of inhibitors revealed its cysteinil-proteinase behaviour.
Biochemical parameters, such as optimum pH, optimum temperature range, thermal stability and protein content of the enzyme preparation were assessed.
Acetonic powder of the calli was prepared with acetone at – 20°C in a 25% w/v rate.
Extractives obtained by gentle stirring with phosphate buffer pH: 7.0 containing 5 mM EDTA (protein content 0.45 g per 100 g of acetonic powder) showed good thermal stability at moderate temperatures and higher proteolytic activity (tested with azocasein, azocoll and haemoglobin as substrates) at pH: 5.0–6.0. The use of a variety of inhibitors revealed its cysteinil-proteinase behaviour.
Authors
M. Parisi, G. Fernández
Keywords
Garlic, proteases, proteolytic activity
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