Isolation and characterization of a protease from the <Emphasis Type="Italic">Actinidia arguta</Emphasis> fruit for improving meat tenderness |
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| Authors: | Juan Wang Haoming Liu Haili Wang Mingxun Cui Qing Jin Tie Jin Fushun Cui Taihua Cui Chengyun Liang Bumsik Kim Guanhao Li |
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| Affiliation: | 1.College of Agriculture,Yanbian University,Yanji, Jilin,China;2.Food Research Center,Yanbian University,Yanji, Jilin,China;3.Collaborative Innovation Center of Beef Cattle Science and Major Demand for Industrial Technology,Yanbian University,Yanji, Jilin,China;4.School of Food Science,Kyungil University,Gyeongsan, Gyeongbuk,Korea |
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| Abstract: | An protease from Actinidia arguta for improving meat tenderness was purified, characterized from wild A. arguta 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 A. arguta 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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