• Food Science of Animal Resources
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• v.18 no.1
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• pp.19-26
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• 1998

In order to study the tenderizing effect of the proteolytic enzyme, ficin, from fig fruit (Ficus carica L), the enzyme was purified from fig latex by precipitation and chromatography. The ficin separated from Bongraesi showed single band on SDS-PAGE. However, the ficin from Masui showed tow bands. The specific activity of ficin purified from Bongraesi species was 2.8 unit/mg protein and that from Masui species was 6.5 unit / mg protein. The amounts of ficin purified from 50 mL of crude latex of Bongraesi and Masui were 1,760 mg and 657 mg, respectively. the water holding capacity of beef decreased to the large extent, when sugar Bongraesi latex and Masui latex were added. The hardness of beef showed decreasing tendency with the time, however, after 60 min, it decreased and thereafter increased a little after 120 min. the hardness of beef decreased sharply with addition of the latex of Bongraesi and Masui. The Masui has more tenderizing effect than the Bongraesi. When meat was mixed with tenderizing agent(ficin) and not heated, the change of color showed significant difference (p＜0.01). when meat was mixed with tenderizing agent(ficin) and heated, the toughness showed significant difference (p＜0.01) and the softness showed significant difference (p＜0.001).

• Food Science of Animal Resources
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• v.44 no.2
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• pp.430-442
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• 2024

This research aimed to assess the effect of collagenolytic proteases from Bacillus subtilis B13 and Bacillus siamensis S6 for tenderizing goat meat during wet aging. Collagenolytic proteases B13 and S6 were prepared at 5 U/mL of collagenolytic activity before injecting into goat meat with 10% (v/w) of initial weight. The control sample was injected with distilled water and used as a negative control. The injected meats were placed in vacuum-sealed bags and wet aged at 4℃ for 0, 3, 5, 7, 14, and 21 days. Thereafter, total aerobic count and physicochemical quality were elucidated. Both enzyme-treated samples from B13 and S6 aged for 5 days showed an acceptable microbial quality with lower than 5.7 Log CFU/g. These conditions produced the tender meats by the reduction in shear force accounting for 30% for B13 and 26% for S6 as compared to the control. Moreover, the enzyme-treated samples showed lower values of hardness, gumminess, and chewiness, with higher springiness and trichloroacetic acid-soluble peptides than the control (p<0.05). The detrimental impact on cooking loss and lipid oxidation was not found. Enzyme-injected meat had a lower cooking loss than the control (p<0.05) with no significant difference in lipid oxidation (p>0.05). Notably, meats treated with B13 and S6 were lower in CIE L^* value as compared to the control (p<0.05) with no significant impact on CIE a^* and CIE b^* (p>0.05). These results suggested that these two collagenolytic proteases could enhance the quality of goat meat in terms of tenderness and reduce the aging time for meat tenderization.

• Food Science of Animal Resources
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• v.31 no.4
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• pp.491-496
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• 2011

The purpose of this study was to examine the effect of a crude protease from Bacillus polyfermenticus on tenderizing pork meat. A B. polyfermenticus protease was characterized, and pork loin samples were treated in solutions containing different enzymes (papain and proteases from Aspergillus oryzae and B. polyfermenticus) and stored for 24, 72, or 168 h at $4^{\circ}C$. Each treated sample was subjected to a quality assessment. B. polyfermenticus protease activity was lower than that for other enzymes tested, although it easily hydrolyzed the meat protein. The optimum temperature and pH for the activity of this protease were $50^{\circ}C$ and pH 7.0. The meat tenderizing activity of the protease from A. oryzae was higher than that of papain and the B. polyfermenticus protease. The fragmentation index of the enzyme-treated with the B. polyfermenticus protease was higher than that of the control. A sensory evaluation was not different between meat treated with proteases, but the overall tenderness of enzyme-treated meats was higher than that of the controls. Therefore, the B. polyfermenticus protease, papain, and the A. oryzae protease appear to be suitable for use as meat tenderizers.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2001.10a
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• pp.22-22
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• 2001

Enzymes have been used in practical applications as diverse as brewing and industrial fermentations, detergent, analytical determinations and recombinant DAN technology. As processing aids, enzymes have been used in the manufacture of food products to improve their quality, solubility and stability for centuries. About 50％ of the enzyme used as industrial processing aids are pretenses which have been used in a number of industrial applications including laundry detergents, chill proofing, meat tenderizing, fermented sauces, and the production of pharmaceuticals. (omitted)

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.3
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• pp.511-519
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• 1999

To prevent the denaturation of ficin(EC 3.4.22.3) that is a proteolytic enzyme in fig(Ficus carica L.), fig conserve was heated to 55oC. The fig conserve was added as a tenderizer to native Korean cattle beef(KCB), dairy cattle beef(DCB), castrated dairy cattle beef(CDCB), and imported beef(IB). The composition of free amino acids, hydroxyproline content, shear force, cooking loss, morphological changes and sensory evaluation were then investigated to observe the effect of tenderizing beef with fig conserve. Free amino acids and cooking loss of treated beef were higher than those of control, whereas hydroxyproline and shear force were lower. Glutamine in treated beef decreased relatively but asparagine increased. Hydroxyproline was found, in increasing order of abundance, in DCB, CDCB, IB and KCB. By portion, loin was higher than tenderloin in free amino acids, hydroxyproline and shear force but was lower in cooking loss. Observation with a light microgram revealed a surprising loss of muscle fiber in treated beef. In sensory evaluation of uncooked beef, the control was redder than the treated beef(p<0.01~p<0.05). Treatment with fig conserve increased the juiciness of both cooked CDCB and IB(p<0.001) and decreased their hardness(p<0.01~p<0.001).

• Proceedings of the Culinary Society of Korean Academy Conference
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• 2005.04a
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• pp.19-42
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• 2005

This study was conducted to investigate the proteolytic properties of Sarcodon aspratus on meat proteins. The analytical condition for the measurement of enzyme activity was determined and the effect of Sarcodon aspratus on beef protein and its fractions were determined by SDS-PAGE and spectrophotometric method, respectively. Optimum temperature and pH of Sarcodon aspratus was $73-78^{\circ}C$,pH 8, respectively. However, the enzyme tended to be denatured at $50^{\circ}C$ for 10min incubation. Proteolytic activity of Sarcodon aspratus was higher than those of kiwi and pear by 66 and 990 times by dry weight, respectively. It was appeared that proteolytic activity of Sarcodon aspratus toward beef protein by SDS-PAGE was prominent when compared to those of kiwi and bromelain. Furthermore, Sarcodon aspratus showed highest proteolytic activity toward all the beef protein fractions, which was followed by collagenase and bovine protease. Transmission electron microscopy showed the muscle fiber started to be degraded when treated with Sarcodon aspratus(1,000 unit) for 10min at $25^{\circ}C$. No distinct sarcomere, A-band, and z-line was observed when treated with Sarcodon aspratus for 60min at same condition.

• Culinary science and hospitality research
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• v.11 no.2
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• pp.110-124
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• 2005

This study was conducted to investigate the proteolytic properties of Sarcodon aspratus on meat proteins. The analytical condition for the measurement of enzyme activity was determined and the effect of Sarcodon aspratus on beef protein and its fractions were determined by SDS-PAGE and the spectrophotometric method respectively. Optimum temperature and pH of Sarcodon aspratus were $73~78^{\circ}C$ and pH 8 respectively. However, enzyme tended to be denatured at $50^{\circ}C$ for 10 min incubation. Proteolytic activity of Sarcodon aspratus was higher than of kiwi and pear 66 and 990 times by dry weight respectively. It appeared that proteolytic activity of Sarcodon aspratus toward beef protein by SDS-PAGE was prominent when compared to that of kiwi and bromelain. Furthermore, Sarcodon aspratus showed the highest proteolytic activity toward all the beef protein fractions, which was followed by collagenase and bovine protease. Transmission electron microscopy showed the muscle fiber started to be degraded when treated with Sarcodon aspratus(1,000 unit) for 10min at $25^{\circ}C$. No distinct sarcomere, A-band, or z-line was observed when treated with Sarcodon aspratus for 60min at the same condition.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.221-228
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• 1975

Meat tenderness is one of the most important factors in meat products because it plays a major role in the palatability of meat. To get information on the role of commercial meat tenderizer, the tenderizing ability of commercial meat tenderizer was measured with various substrates. The results obtained are as follows. 1. Content of crude protein in a commercial meat tenderizer was 4.9%. 2. Optimum temperature for proteolytic activity of meat tenderizer was $60{\sim}70^{\circ}C$. 3. Maximal activity of proteinase was obtained at pH $6{\sim}7$. 4. Proteolytic enzyme was activated by KCN, NaCN, EDTA. Thus, it was concluded that protease system of commercial meat tenderizer composed of plant origin proteinases. 5. Proteinase activity was completely inhibited by 10mM of N-Ethylmaleimide. 6. Commercial meat tenderizer showed stronger proteolytic activity on casein than on the water soluble fraction of meat protein, whereas it hydrolyzed the myofibrillar protein less efficiently.

• Food Science of Animal Resources
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• v.36 no.1
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• pp.114-121
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• 2016

This study was performed to improve the techniques used for tenderizing red meat as elderly food. Beef meat was immersed in liposome encapsulated enzyme solution and the effect of protease encapsulation on the beef properties was analyzed. The protease encapsulation properties were analyzed according to the size distribution and enzymatic activity. After enzyme reaction on the beef, the chemical properties of the meat such as pH, water holding capacity, shear rate, lipid oxidation and total volatile basic nitrogen (TVB-N) were analyzed. The pH of the beef increased during the reaction and coating protease (CP) was higher than non-coating protease (NCP). Total color differences were increased remarkably after 36 h and generally, the difference in CP was relatively lower than in NCP. WHC was significantly decreased within 24 h, and no effect from the protease coating was observed. Protease activity was significantly increased within 48 h and no differences in the enzyme coating were observed. The TVB-N value of NCP was increased within 24 h while CP was sustained for up to 36 h. The TVB-N value of protease treated meat increased after 36 h and no effect from the protease coating was detected. Consequently, liposome encapsulated protease was found to have similar properties as non-coated protease. Application of liposome seems to be an interesting option for injecting various functional materials without changing the properties of meat.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.6
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• pp.1027-1031
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• 1994

A method for the process of making fig conserves to prevent the denaturation of ficin (EC3.422.3) that is a proteolytic enzyme in fig (Fixus carica L. ) has been developed. The suutable composition ratio of materials such as, fig, sugar, citric acid and potassium sorbate, to make fig conserves was 1,000, 600 , 1.0 and 0.67g , respectively. to maintain the ficin activity, it was necessary that these materials were heated on 55$^{\circ}C$ and concentrated in the reduced pressure. At a result of sensory evaluation , meat treated with fig was the softest among samples. Then the treated beef with 55$^{\circ}C$ converse, 7$0^{\circ}C$ conserves, sugar and control have been shown the decreased rate respectively. There was significantly different in the effect of tenderness between each group(0.1%) . The nitrogen content of connective tissue was relatively low in the groups of the treated beef with fig and 55$^{\circ}C$ converses, 7$0^{\circ}C$ converses sugar and control , which was similar to the order of the ficin activity. This research revealed that the constituent protein of meat muscle was decomposed by ficin and its solubility was relatively higher than before.