• Applied Biological Chemistry
• /
• v.30 no.3
• /
• pp.210-218
• /
• 1987

In the previous report, we isolated and purified one of tendering enzyme 'ficin' from fig latex. In this study, various crude ficin concentrations and reaction time were employed to investigate the contents of free amino acids and other free nitrogen compounds after the treated with beef round muscle. 1. Free amino acids contents increased with the increase of temperature and time during the aging of beef at $1^{\circ}C$ and $8^{\circ}C$, and the increasing rate was remarkably high when fresh beef was treated with ficin. In the case of ficin treatment after various cooking, steaming showed the highest increase in free amino acid contents among three cooking methods such as boiling, steaming and pan broiling. The increased amounts of free amino acids in three groups-aging beef at $1^{\circ}C$ for 3 days, fresh beef treated with ficin(0.1%, 2hrs) and beef treated with ficin(0.1%, 2hrs) after cooking were 13%, 293% and 137% respectively. In contrast to aging group, the amount of free amino acids in other two groups treated with ficin was superiorly increased. 2. The amounts of total free nitrogen, free non-protein nitrogen and $NH_3-nitrogen$ increased with the increase of temperature and time during the aging of beef at $1^{\circ}C$ and $8^{\circ}C$, and the increasing rate was remarkably high in fresh beef treated with ficin. In the case of ficin treatment after cooking, steaming gave larger amount of total and non-protein nitrogen than other two cooking, e.g. boiling and panbroiling. The increasing rate of nonprotein nitrogen to the total nitrogen of fresh beef treated with ficin(0.1%, 2hrs) was 75 times greater than that of aging fresh beef at $1^{\circ}C$ for 3 days.

• Korean Journal of Food Science and Technology
• /
• v.18 no.4
• /
• pp.270-277
• /
• 1986

Ficin, a proteolytic enzyme in Fig latex, was extracted and purified with using ammonium sulfate and CM-cellulose column chromatography, respectively, and studied for its chemical properties. The disc gel electrophoresis showed one major and three minor bands for $(NH_4)_2SO_4$ extract and only one band showed after CM-cellulose chromatography. The optimum conditions for ficin activity was found to be pH 7.0 and $50^{\circ}C$. The amino acids composition of the purified ficin were 21.8% as acidic, 3.5% as basic and 74.7% as neutral amino acids. The amino acids analysis indicated that the ficin was composed of 174 amino acids residue having molecular weight of 19,500.

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

• The Korean Journal of Food And Nutrition
• /
• v.2 no.2
• /
• pp.21-26
• /
• 1989

The morphological changes of fresh beef treated with ficin(0.1% : 2 hrs, 6 hrs)were examined with transmission electron microscope(TEM), the results obtained were as follows ; Connective tissue protein in fresh beef treated with ficin became gradually fragmentation and was occurred solubilization with time The length of sarcomere in myofibrillar protein was elongated, M-line became dim, and the 1-band of Z-line was broken and beck me fragmentation with time.

• The Korean Journal of Food And Nutrition
• /
• v.1 no.2
• /
• pp.1-8
• /
• 1988

The morphological changes of fresh beef treated with ficin(0.1% : 35$^{\circ}C$ 2hrs, 6hr,) were examined with scanning electron microscope(SEM), the results obtained were as follows ; Connective tissue protein in fresh beef treated with ficin was occurred solubilization with time and gradually trasformed from a definite form into amorphous form, followed by showing an opening-up phenomenon again and subdivision. Myofibrillar protein was cracked and breaked slightly, followed subdivision with time.

• The Korean Journal of Food And Nutrition
• /
• v.1 no.2
• /
• pp.9-17
• /
• 1988

The morphological changes of fresh beef treated with ficin(0.1% : 2hrs, 6hrs) were examined with optical microscope (OM, LM), the results obtained were as follows : Connective tissue protein in fresh beef treated with ficin was occurred swelling and separation of endomysial reticulum with time, followed showing granulation and solubilization slightly. Myofibrillar protein was loosed wavy contractile muscle fiber, and showed erosin, cracks and breaks in fibers with time.

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

• Korean Journal of Food Science and Technology
• /
• v.24 no.1
• /
• pp.101-106
• /
• 1992

Vie investigated the clarification effects of foxtail millet wine, a traditional wine in Cheju island, by centrifugation, protease treatment and ultrafiltration(UF). It was difficult to remove completely cloudy substances in foxtail millet wine only by centrifugation. With protease concentration of $5{\times}10^{-4}%(w/v)\;at\;35^{\circ}C$, for 2 hrs, foxtail millet wine was clarified effectively. Papain and bromelain appeared similar effects to the clarification of wine, but ficin was inferior to those. Ultrafiltration with pore size $100K\;and\;0.22{\mu}m$ membranes had appeared better clarification effects than the best result of enzyme treatment, and then was considered as a simple and economic method.

• Korean Journal of Food Science and Technology
• /
• v.27 no.5
• /
• pp.794-798
• /
• 1995

Deamidation by neutrase on glutaminyl and asparaginyl residues of protein was examined. The optimum pH and temperature for BSA(bovine serum albumin) deamidation by neutrase were 10 and $20^{\circ}C$, respectively. The incubation for 3 hrs under the optimum condition removed 24% of amide groups and hydrolyzed 2.9% of peptide bonds. Deamidation by neutrase was superior to that by pronase, bromelain, or ficin. Deamidation degrees of egg albumin, soy protein isolate and casein by neutrase under the optimum condition were about 20%, 14% and 14%, respectively. However, relatively high degree of peptide hydrolysis was accompanied with casein deamidation.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.19 no.1
• /
• pp.20-26
• /
• 1986

Very little information is available in the literature on storage of fish sauce. Therefore, microbiological and chemical chracteristics during storage and quality of fish sauce were investigated and discussed to present data about the optimum storage condition. The chopped sardine meat was mixed with equal amount of water and $9\%$(w/w) of $75\%$ vital wheat gluten and then hydrolyzed by addition of commercial proteolytic enzymes such as bromelain, papaya protease, ficin and a enzyme mixture (Pacific Chem. Co.) for 4 hours at $52.5^{\circ}C$. The reaction mixture was heated for 30 min at $100^{\circ}C$ for enzyme inactivation, pasteurization and color development and then centrifuged for 20 min at 4,000 rpm. Table salt and benzoic acid were added for bacteriostatic effect and stored for 80 days at $15{\pm}1^{\circ}C$ and $30{\pm}1^{\circ}C$. The results were summarized as follows: 1. The amount of amino-nitrogen and pH of fish sauce were almost unchanged during storage. 2. Mininum concentration of salt for bacteriostatic activity was $9\%$(w/w) regardless of addition of benzoic acid. 3. the yields of amino-nitrogen were $63.1\%$ for the hydrolysate prepared without enzyme, $79.7\%$ for that with bromelain, $69.9\%$ with ficin, $74.3\%$ with papaya pretense, and $78.1\%$ with enzyme mixture, respectively. 4. The contents of amino-nitrogen were $4510.0mg\%$ on the dry basis for the product prepared by autolysis, $5483.2mg\%$ for that prepared with bromelain, $5305.7mg\%$ with ficin, $4994.1mg\%$ with papaya protease and $5582.3mg\%$ with the enzyme mixture, respectively. 5. The contents of crude protein were $51.35\%$ on the dry basis for the product prepared by autolysis and 55 to $59\%$ for prepared with commercial enzymes. 6. The hydrolysate prepared with the enzyme mixture revealed a little stronger meaty taste than any other products. 7. The level of crude protein in residues was still high ($69.5{\sim}77.2\%$ on the dry basis) and might be originated from the added vital wheat gluten.