In vitro analysis of mushroom proteases that may tenderize beef
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Date
2018-04-03
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Abstract
Meat tenderness is an important characteristic that influences consumer purchasing decisions. Protease extracts from pineapple, ginger, papaya and kiwi have exhibited proteolytic activity to tenderize meat products. Unfortunately, many of these proteases have broad activity that can overtenderize the meat and negatively affect texture and quality. Therefore, identification and evaluation of other proteases capable of tenderizing beef is necessary. Previously, mushrooms have been shown to enhance flavor and nutritional composition of meat dishes, as well as having beneficial antioxidant and health effects. Mushrooms also contain a variety of proteases that were analyzed in this study for their ability to denature beef proteins using an in vitro model system. Eight mushroom varieties were tested including white button (white immature Agaricus bisporus), crimini (brown immature Agaricus bisporus), portobello (mature Agaricus bisporus), shitakke (Lentinula edodes), enoki (Flammulina velutipes), oyster (Pleurotus ostreatus), king trumpet (Pleurotus eryngii), and brown beech (Hypsizygus tessellatus). Mushrooms were homogenized in a 20 mM Tris buffer (pH 8.0), filtered, then centrifuged. Afterward, purified bovine myofibrils were combined with the crude mushroom protease extracts and incubated at 25°C. Samples were collected at 0, 30, 60, 240, and 1440 min. After, myofibrillar proteins were solubilized and separated using SDS-PAGE. Density of protein bands were quantified and compared between the time-points. The data indicated that all eight mushroom varieties proteolyzed myofibrillar proteins including actin and myosin. Therefore, these results support the possibility that mushroom proteases may be able to tenderize beef, forming the basis for future research trials.
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Food Science, Safety, & Security (The Ohio State University Denman Undergraduate Research Forum)
Keywords
Mushroom, Proteases, Tenderize, Beef, In vitro, SDS-PAGE