Actinidin: A Promising Milk Coagulating Enzyme
Masoud Alirezaei, Mahmood Aminlari, Hamid Reza Gheisari, Maryam Tavana
European Journal of Nutrition & Food Safety · pp. 43–51 · Published 22 Mar 2011
Abstract
The aim of this work was to study proteolytic activity of actinidin in comparison with chymosin and ficin on bovine milk substrate. The specific activities of purified ficin and actinidin were 7.9 and 8.3 unit/mg protein, respectively. The optimum clotting activity of both actinidin and ficin was at 45°C, although chymosin was relatively less sensitive to temperature. Increasing CaCl2 concentration resulted in an enhancement of the clotting activities of all coagulating enzymes, this effect noticeable for ficin. In ficin treated sample significant decrease of bands intensity in the range 25-30 KD and appearance of some of κ-casein in 20 KD regions was observed by using SDS-PAGE. In conclusion, the chymosin and actinidin gave similar relative activity at different temperatures, pH values and CaCl2 concentrations for bovine milk substrate. Comparable electrophoresis profile of actinidin, ficin and chymosin by analysis of the whey with SDS-PAGE indicates that actinidin could be a potential alternative for chymosin.
Cited by 0
No indexed citations yet.
Related research
- Isolation and Purification of an Antifungal Protein from Kiwi Fruits and Demonstration of Its Antifungal Activity — shares topic coverage
- Comparative Analysis of Soxhlet and Ultrasound-assisted Extraction of Bioactive Components from Fig Leaves (lat. Ficus carica): Impact of the Method on Extraction Yield and Latex Preservation — shares topic coverage
Article metrics
Real usage data collected on this platform.
0
Page views
0
PDF downloads
0
Outbound clicks
0
Citations
Views by country
Approximate, from request IP at view time — not citizenship or institution. Countries with fewer than 5 views are grouped as "Other".
No views recorded yet.
Traffic sources
Referring site, by host.
No traffic recorded yet.
Views and downloads exclude known bots/crawlers. Citations combines this platform's own DOI-resolved index with each external source's own reported total — see Cited by above for individually listed citing works. Last refreshed 0 seconds ago.