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Improving Meat Tenderness by using Protease Extract from Paddy Oats (Gnetum gnemon) Fruit Peel
( Cahyo Indarto ),( Shyang-chwen Sheu ),( Pomin Li ) 한국농업기계학회 2018 한국농업기계학회 학술발표논문집 Vol.23 No.1
This study investigated the possibility of an agricultural waste, paddy oats (Gnetum gnemon L.) fruit peel, as a source of protease extract, particularly used as a meat tenderizer. The effect of paddy oats protease extract on meat tenderness was evaluated and compared to those of commercial papain, commercial bromelin, and control. Paddy oats protease extract showed the high meat tenderizing activity since it resulted in shear force value of meat sample 46% lower than that of control, and similar (p<0.05) with those of commercial papain and commercial bromelin. Panelists scored the meat sample treated with paddy oats protease extract much more tender (7.4) than that of control (5.8), using a 10 point hedonic scale and no different (p<0.05) from those of commercial papain and commercial bromelin with score 7.3 and 7.7, respectively. Paddy oats protease extract also consistently ranked high for all evaluated parameters, therefore paddy oats protease extract could have a high potential as a meat tenderizer for improving tenderness quality of meat.
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Yi-Yang Lien,Chi-Hung Huang,Fang-Chun Sun,Shyang-Chwen Sheu,Tsung-Chi Lu,Meng-Shiunn Lee,Shu-Chin Hsueh,Hsi-Jien Chen,Meng-Shiou Lee 대한수의학회 2012 JOURNAL OF VETERINARY SCIENCE Vol.13 No.1
Chicken anemia virus (CAV) is an important viral pathogen that causes anemia and severe immunodeficiency syndrome in chickens worldwide. In this study, a potential diagnostic monoclonal antibody against the CAV VP1 protein was developed which can precisely recognize the CAV antigen for diagnostic and virus recovery purposes. The VP1 gene of CAV encoding the N-terminus-deleted VP1 protein, VP1Nd129, was cloned into an Escherichia (E.) coli expression vector. After isopropyl-b-D-thiogalactopyronoside induction, VP1Nd129 protein was shown to be successfully expressed in the E. coli. By performing an enzyme-linked immunoabsorbent assay using two coating antigens, purified VP1Nd129 and CAV-infected liver tissue lysate, E3 monoclonal antibody (mAb) was found to have higher reactivity against VP1 protein than the other positive clones according to the result of limiting dilution method from 64 clones. Using immunohistochemistry, the presence of the VP1-specific mAb, E3, was confirmed using CAV- infected liver and thymus tissues as positive-infected samples. Additionally, CAV particle purification was also performed using an immunoaffinity column containing E3 mAb. The monoclonal E3 mAb developed in this study will not only be very useful for detecting CAV infection and performing histopathology studies of infected chickens, but may also be used to purify CAV particles in the future.
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