Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins

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• 作者：Minh Ha^a ; ^b ; Alaa El-Din A. Bekhit^b ; ^{aladin.bekhit@otago.ac.nz} ; Alan Carne^a ; David L. Hopkins^c
• 关键词：Meat ; Proteases ; Characterisation ; Plant ; Proteins
• 刊名：Food Chemistry
• 出版年：2012
• 期刊代码：48_03088146
• 类别：abs
• 出版时间：1 September, 2012
• 卷：134
• 期：1
• 页码：95-105
• 文件大小：1006 K

摘要

Four commercially available plant preparations containing respectively papain, bromelain, actinidin and zingibain were evaluated for their ability to hydrolyse proteins present in both beef connective tissue and topside myofibril extracts. The results show significant differences in protease activity depending on the assay used and that protease assays with connective tissue and meat myofibril extracts provide a realistic evaluation of the potential of the enzymes for application in meat tenderisation. The actinidin protease preparation was found to be most effective at hydrolysing beef myofibril proteins and the zingibain protease preparation most effective at hydrolysing connective tissue proteins. This indicates the potential of these proteases for targeting specific tenderising applications, in contrast to trying to achieve control of tenderisation with the more active papain and bromelain proteases.