An protease from for improving meat tenderness was purified, characterized from wild fruit by ammonium sulfate precipitation, Sephdex G-25 gel filtration chromatography, and DEAE Sepharose Fast Flow ion exchange chromatography, and its activity was investigated. The purified protease was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis to obtain a single band of protease. The protease was purified successfully, and found to have a molecular weight of 23.8 kDa (mass spectrometry). The specific activity of the purified protease reached 53,428 U/mg with a 25.5-fold purification factor and 9% activity recovery. Based on N-terminal sequencing results, the protease was derived from the class of actinidia proteases that have an N-terminal sequence of VLPDY VDWRS AGAVV. The protease was effective for tenderizing beef and decomposing actomyosin, suggesting the potential application for improving meat tenderness.
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| http://dx.doi.org/10.1007/s10068-016-0171-y | DOI Listing |
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