Characterisation of novel fungal and bacterial protease preparations and evaluation of their ability to hydrolyse meat myofibrillar and connective tissue proteins. (1st April 2015)

• Record Type: Journal Article
• Authors: Ryder, Kate; Ha, Minh; Bekhit, Alaa El-Din; Carne, Alan
• Is Part Of: Food chemistry. Volume 172(2015)
• Page Start: 197
• Page End: 206
• Publication Date: 2015-04-01
• Subjects: Meat -- Myofibrillar -- Connective tissue -- Fungal proteases -- Tenderisation; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2014.09.061
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Catalytic properties of one bacterial and three fungal proteases were compared. Proteases demonstrated different activities towards different substrates. AFP and HT showed the fastest hydrolysis of myofibrillar extract. All four proteases showed potential to hydrolyse connective tissue extract. Abstract: The catalytic capability of four commercially available food-grade fungal and bacterial protease preparations (AFP, FPII, F60K and HT) was evaluated over a range of pH, temperature and substrate conditions using esterase and caseinolytic activity assays and time course hydrolysis over 120 and 60 min of myofibrillar and connective tissue proteins, respectively. The protease preparations displayed similar casein hydrolysis kinetics and were active in hydrolysing BODIPY-FL casein to varying extents at postmortem aging meat pH (5.0–6.0). All of the four proteases exhibited selective hydrolytic activity towards meat myofibrillar proteins including myosin and actin. Significant hydrolysis of two meat tenderisation protein markers troponin T and desmin by the four proteases was detected by western blot. The results obtained indicate that the new fungal protease preparations AFP and FPII, bacterial protease preparation HT and the new source of fungal protease preparation F60K have potential for use in meat tenderising applications.