• Title/Summary/Keyword: ficin

검색결과 22건 처리시간 0.024초

Ficin 처리 우육의 소화에 관한 연구 (Studies on the Digestion of Beef by Ficin Treatment)

  • 김정숙;김준평
    • Applied Biological Chemistry
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    • 제30권3호
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    • pp.210-218
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    • 1987
  • 전보에서 무화과 latex에서 ficin을 분리 정제한 바 있다. 본 연구에 있어서 조 ficin을 우육에 처리하여 그의 연육제로서의 단백질 분해효과를 살피기 위하여 ficin을 농도별로 우육에 작용했을 때 생기는 유리아미노산 및 질소화합물의 함량을 측정 하였으며 이들을 숙성 및 조리시의 함량과 비교검토하였으며 그 결과는 다음과 같다. 유리 아미노산의 함량은 $1^{\circ}C$$8^{\circ}C$에서 숙성시 처리온도 및 시간에 따라 증가하였고 생우육에 ficin 처리시는 더욱 증가하였으며 증가율 또한 현저하게 높았다. 조리후 ficin 처리의 경우는 "삶기", "찌기", "굽기"의 경우중 찌기가 유리아미노산이 가장 많이 증가하였으며 또한 아미노산 증가량은 숙성중($1^{\circ}C$, 3일) 생육에 ficin 처리 (0.1% 8시간) 조리후 ficin 처리(0.1% 2시간)을 비교하였을 때 각각 13%, 292%, 137%로서 ficn 처리시의 두 group이 숙성중인 것보다 월등히 증가하였다. 총질소, 비단백태질소 및 암모니아태질소의 함량 변화는 $1^{\circ}C$$8^{\circ}C$에서 숙성시 처리온도와 시간에 따라 증가하였으며 생우육에 ficin 처리시는 더욱 증가하였으며 그 증가율이 현저하게 높았다. 조리후 ficin의 처리 경우에는 "삶기", "찌기", "굽기"의 경우에서 "찌기"가 암모니아태질소를 제외하고는 그 수치가 가장 높았다. 또한 숙성중($1^{\circ}C$, 3일)인 생육과 ficin 처리시의 생육의 총질소에 대한 비단백태질소의 증가율을 비교하였을 때 ficin 처리한 생육이 숙성중인 생육보다 크게 증가하였다.

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무화과(無花果)에서 Ficin의 분리(分離) 및 정제(精製) (Isolation and Purification of Ficin from Fig Latex)

  • 김준평;서재신;김정숙
    • 한국식품과학회지
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    • 제18권4호
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    • pp.270-277
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    • 1986
  • Ammonium sulfate 염분획과 CM-cellulose chromatography로 Fig latex에서 ficin을 분리하여 다음과 같은 결과를 얻었다. 분리한 crude ficin을 전기영동한 결과 main band 와 3개의 minor band로 나타났으며 main peak의 정제에서 얻은 ficin은 단일 band로 나타났다. 분리한 ficin의 pH 및 열에 대한 영향을 PH7.0, $60^{\circ}C$에서 최적 작용을 나타내었다. 분리한 ficin의 pH에 대한 안정성은 pH $2{\sim}8$로 비교적 넓은 범위로 나타났고 열에 대한 안정성은 $0{\sim}55^{\circ}C$의 범위로 안정성이 나타났다. 분리한 ficin의 분자량은 19500으로 나타났다. 산성 아미노산 21.8%. 염기성 아미노산 3.5%, 중성아미노산74.7%로 나타났으며 cystine과 tryptophan을 제외한 아미노산 잔기수는 174로 나타났다.

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무화과 단백질 분해효소의 식품에의 이용 (Application of Fig Protease to Foods)

  • 기해진;황영선;김강화;홍윤호
    • 한국축산식품학회지
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    • 제18권1호
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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).

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Ficin 처리시 우육의 단백질 분해에 관한 연구 V. 투과형 전자현미경에 의한 관찰 (Studies on the Digestion of Beef by Ficin Treatment V. A Transmission Electron Microscopic Observation)

  • 김정숙
    • 한국식품영양학회지
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    • 제2권2호
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    • pp.21-26
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    • 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.

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Ficin처리시 우육의 단백질 분해에 관한 연구 III. 주사형 전자 현미경에 의한 관찰 (Studies on the Digestion of Beef by Ficin Treatment : III. A Scanning Electron Microscapic Observation)

  • 김정숙
    • 한국식품영양학회지
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    • 제1권2호
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    • pp.1-8
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    • 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.

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Ficin처리시 우육의 단백질 분해에 관한 연구 IV. 광학 현미경에 의한 관찰 (Studies on the Digestion of Beef by Ficin Treatment : IV. An Optical Microscopic Observation)

  • 김정숙;주순재
    • 한국식품영양학회지
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    • 제1권2호
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    • pp.9-17
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    • 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.

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연육용 무화과 잼 개발 연구 -쇠고기 연화용 무화과 콘서트 (Fig Conserves) 개발 연구- (A Study on the Manufacturing of Gig Conserves for Beef Tenderizing)

  • 박복희;박원기
    • 한국식품영양과학회지
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    • 제23권6호
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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.

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좁쌀약주의 청징화 (Clarification of Foxtail Millet Wine)

  • 김효선;양영택;정용현;고정삼;강영주
    • 한국식품과학회지
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    • 제24권1호
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    • pp.101-106
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    • 1992
  • 제주도 전통주인 좁쌀약주를 청징화시키기 위하여 원심분리에 의한 청징화 방법, 단백효소제(papain, bromelain, ficin)에 의한 청징화 방법과 한외여과에 의한 청징화 방법들을 검토하여 좁쌀청주의 가장 효과적인 청징화 방법을 모색하고자 하였다. 원심분리에 의해서만은 혼탁물질의 완전한 제거는 불가능하였으며, 단백효소제를 이용한 경우에서는 효소농도 $5{\times}10^{-4}%(w/v)$ 작용시간 2시간, 작용온도 $35^{\circ}C$에서 매우 우수한 청징효과를 나타냈다. 효소별 청징도는 papain과 bromelain은 거의 비슷한 효과를 보였으나, ficin의 청칭력은 약간 떨어졌다. 한외여과(여과막 크기 100k와 $0.22{\mu}m$막)에 의한 청징화는 효소에 의한 최고의 청징화 수준보다 약간 우수한 청징효과를 보였으며, 효소처리에 비하여 향미성분의 손실이나 색도가 좀더 나아서 UF에 의한 청징화 방법이 간단하고 경제적인 방법이었다.

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Neutrase에 의한 glutamine과 aspargine 잔기의 탈아미드화 (Deamidation on Glutaminyl and Asparaginyl Residues of Protein by Neutrase)

  • 김효선;강영주
    • 한국식품과학회지
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    • 제27권5호
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    • pp.794-798
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    • 1995
  • 식품단백질의 효율적인 이용을 위하여 neutrase에 의한 glutamine과 asparagine 잔기의 탈아미드화에 관한 연구를 행하였다. Neutrase에 의한 BSA의 최적반응 조건은 $20^{\circ}C$, pH 10에서 3시간 반응시켰을 때로, 이때 BSA는 24%가 탈아미드화되었고. 동시에 2.9%가 가수분해되었다. 또한 pronase, bromelain, ficin 보다는 neutrase에 의한 BSA의 탈아미드화율이 높은 것으로 나타났다. 최적 탈아미드화 조건에서 neutrase에 의한 egg albumin, 분리콩단백 및 casein의 경우 탈아미드화에 수반하여 펩티드결합의 분해가 비교적 높게 관찰되었다.

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어장유의 품질과 저장안정성 (Qualify and Stability of Fish Sauce during Storage)

  • 김병삼;박상민;최수일;김장양;한봉호
    • 한국수산과학회지
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    • 제19권1호
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    • pp.20-26
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    • 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.

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