Identification and Functional Characterization of Cysteine Protease from Nine Pear Cultivars (Pyrus pyrifolia) |
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Authors: | Seung-Hee Nam Marie K Walsh Su-Hyun Kim Kwang-Yeol Yang |
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Affiliation: | 1. Functional Food Research Center, Chonnam National University, Gwangju, Republic of Korea;2. Department of Nutrition, Dietetics, and Food Sciences, Utah State University, Logan, Utah, USA;3. Department of Plant Biotechnology, College of Agriculture and Life Sciences, Chonnam National University, Gwangju, Republic of Korea |
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Abstract: | This study was performed to compare the total protein and protease content among the whole fruit, flesh, and peel of nine different pear cultivars. Pear proteases were functionally characterized with respect to three enzyme assays. Proteases from pears were further identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, in gel activity staining, and matrix assisted laser desorption/ionization-time of flight mass spectrometry analysis. Flesh from Whasan, Nikita, and Hanareum cultivars contained relatively more total protein and protease and showed high enzyme activities, while Chuwhang contained the lowest amount of protein and protease activity. Protease content and enzyme activities found in the pear flesh or whole fruits were two to six times higher than those in the pear peel. Pear cultivars contained one or two protease bands with molecular weights of 36 kDa and/or 38k Da. The larger band was further identified as a cysteine proteinase with 70% homology to the pear cysteine protease from Pyrus pyrifolia. |
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Keywords: | Pear cultivars Cysteine protease Functional characterization |
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