• 한국식생활문화학회지
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• 제23권4호
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• pp.514-520
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• 2008

This study addresses the development of a soy hamburger patty containing enzyme-treated textured soy protein (TSP) as a meat analogue. In order to reduce the beany flavor and enhance the texture, TSP was treated with 0.3% Flavourzyme for 5, 10, 20, or 30 min. The degree of hydrolysis and the water holding capacity of the TSP increased with increasing hydrolysis time. The oil binding capacity of the TSP also increased with increasing hydrolysis time, approaching the maximal value, 175.82%, at 30 min, whereas that of pork scored with the lowest value of 128.67%. The volume of pork was reduced to 81.5% as the result of heat treatment, whereas that of the TSP increased to 140.57%. The values of 'L', 'b', and '${\Delta}E$' differed significantly (p<0.001) with heat treatment, but the 'a' values did not differ significantly. With regard to texture, the hardness values were highest in the pork hamburger patty (PHP), and were lowest in the soy hamburger patty (SHP) containing untreated TSP. The hardness of the SHP containing TSP treated for 20 min did not differ significantly from that of the PHP. The cohesiveness and gumminess of the SHP treated for 20 min were highest, whereas those treated for 10 min were the lowest. The gumminess of the SHP treated for 20 min did not differ significantly from that of pork. The chewiness of the PHP was the highest, whereas that of the SHP treated for 5 min was the lowest. In our sensory evaluation, PHP evidenced the highest scores, followed by the SHP treated for 30 min, as color, texture, beany flavor, and overall quality all improved as the consequence of increasing enzyme treatment duration. In conclusion, it is believed that SHP has great potential as a substitute for meat, in that the flavor, texture, and beany flavor of SHP did not differ significantly from those of PHP.

• Journal of Pharmaceutical Investigation
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• 제19권4호
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• pp.203-212
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• 1989

A proteolytic enzyme was extracted from Sarcodon aspratus (Berk) S. Ito by percolation method. Proteolytic activity of the extracted proteolytic enzyme (SAP) was compared with several digestives containing proteolytic enzymes. Potency of SAP was higher than that of the other digestives except for protease. The optimum pH ranse of SAP was similar to that of pancveatin and protease. SAP was more stable than pancreatin and protease under various temperature, alkaline pH, and metal ions. Bovine serum albumin hydrolysing activity of SAP was equivalent to that of pancreatin and protease in small intestine of rats. SAP demonstrated lower adsorption to antacids than pancreatin and protease. Among the mixtures of SAP and several antacids, magnesium oxide-SAP showed the highest proteolytic activity.

• Journal of the Korean Wood Science and Technology
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• 제19권2호
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• pp.22-29
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• 1991

The endo-1,4-${\beta}$-xylanase was extracted and purified from the extracellular xylanolytic systems of Trichoderma viride. The crude enzyme was chromatographed with ion-exchange reins of DEAE Sepharose CL-6B, Sepharose, S-Sepharose CL-6B and the resulting xylanase was turned out to be a single protein as 20KD hy SDS-polyacrylamide gel electrophoresis. The xylooligomers were obtained from xylan by incubation with the purified xylanase up to 50%. The ${\beta}$-xylosidase lost its activity completely by incubation of crude enzyme for 24hr with buffer solution of pH 2.8 at $27^{\circ}C$. And also, the xylooligomers were obtained from xylan as a main product by incubation with the crude enzyme treated with acidic buffer.

• 한국펄프종이공학회:학술대회논문집
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• 한국펄프종이공학회 1999년도 Proceedings of Pre-symposium of the 10th ISWPC
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• pp.149-152
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• 1999

A new process for deinking of colored offset newsprint, i.e. enzyme treatment in cooperation with ultrasonic wave was developed in the present study. The physical characteristics such as fiber length, coarseness, crystallinity index of the deinked pulps were investigated and the sugar residues released from the treatment were analyzed. It was found that colored offset newsprint could be deinked effectively by cellulase treatment when ultrasonic wave was applied. The brightness increased by 5% ISO over that of control experiment and the pigment content was reduced markedly. Though the ultrasonic wave had little effect on the strength and crystallinity of the pulp, the treatment of enzyme combined with ultrasonic wave reduced the coarseness and fiber length to some extent. It was also found that ultrasonic wave could accelerate the hydrolysis of cellulose and hemicellulose during the cellulase treatment.

• 한국식품영양학회지
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• 제7권1호
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• pp.16-22
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• 1994

Xylanase from Bacillus sp. GS was purified through acetone precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel filtration. The optimum reaction temperature of purified xylanase was 50t . Its optimum pH was between pH 6.0 and pH 6.5. This enzyme was stable below 5$0^{\circ}C$ for several hours and stable at between pH 5.5 and pH 8.0. The enzyme activity of xylanase was remarkably increased by Co++ and Cu++ ions. According to the study of hydrolysis mode of this enzyme, it was turned out to be ends type xylanase that can produce xylooligosaccharides, known as bifidogenic factor, from xylan.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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• pp.35-35
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• 1999

Amylases catalyze the hydrolysis of starch material and play central roles in carbohydrate metabolism. The structure and a size exclusion column chromatography proved that the enzyme is a dimer in solution. The N -terminal segment of the enzyme folds into a distinct domain and comprises the enzyme active site together with the central (${\alpha}$/ ${\beta}$)$\sub$8/ barrel of the adjacent subunit.(omitted)

• 한국미생물·생명공학회지
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• 제18권1호
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• pp.39-43
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• 1990

본 저해물질은 10Mug의 Alpha-D-glucosidase에 대해서 50Mug 및 100Mug을 첨가했을 때 저해율은 각각 60, 80 정도였으며 enzyme-inhibitor complex를 비교적 서서히 형성하여 5분간 진처리하였을 때 약 55의 저해율을 나타내었다. 그리고 Alpha-D-glucosidase, Alpha-galactosidase및 Beta-galactosidase를 제외한 탄수화물 분해효소에 대해서는 저해능이 없었으며, Alpha-D-glucosidase에 대한 저해양상은 non-competitive type 이었으며 Ki 값은 118 $\mu$g/m$\ell$였다.

• 한국식품영양과학회지
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• 제39권1호
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• pp.8-13
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• 2010

분리대두단백질의 가수분해물을 제조 시, 최적 가수분해 조건을 설정하기 위하여 총 7종의 단백질 가수분해 효소를 이용하여 효소선정, 효소농도, 가수분해시간 및 분리대두단백질분말의 첨가량에 따른 단백질의 함량 정도를 나타내는 280 nm의 흡광도 측정과 수율을 대신한 brix 측정, 가수분해물의 ACE 저해활성 등을 조사하였다. 분리대두단백질 분말에 증류수를 5%의 분산농도로 하여 분해효소 Alcalase 2.4 L을 1%(v/w) 첨가하여 $65^{\circ}C$에서 4시간 동안 가열하여 가수분해하였다. 가수분해를 마친 후 효소의 반응정지를 위하여 $80^{\circ}C$에서 5분간 열처리한 후, $4^{\circ}C$로 냉각하여 원심분리(7,000 rpm, 40 min) 하였다. 원심분리 한 상등액을 취하여 여과한 후, $60^{\circ}C$에서 농축하였다. 농축액을 냉동시켜, 진공 동결건조 하여 분리대두단백질 가수분해물을 제조하였다. 분리대두단백질 가수분해물의 수율은 38.32%를 나타냈으며, ACE 저해활성($IC_{50}$)은 $79.94 {\mu}g/mL$를 나타내었다.

• Journal of Microbiology and Biotechnology
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• 제11권5호
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• pp.845-852
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• 2001

A microorganism producing fibrinolytic enzyme was isolated from Korean traditional soybean paste and identified as Bacillus sp. KDO-13. The fibrinolytic enzyme was purified to homogeneity by ammonium sulfate fractionation, ion-exchange chromatography on DEAE-celluose, and gel chromatography on Sephadex G-100 of the culture supernatant of Bacillus sp. KDO-13. The molecular weight of the purified enzyme was estimated to be 44,000 by SDS-PAGE. The optimum pH and temperature for the enzyme activity were pH 8.0 and $50{\circ}C$, respectively. The enzyme activity was relatively stable at pH 7.0-9.0 and temperature below $50{\circ}C$. the activity of the enzyme was inhibited by $AI^{3+}$ and $Hg^{2+}$, but activated by $Co^{2+}$\;and\;Ni^{2+}. In addition, the enzyme activity was potently inhibited by EDTA and 0-phenanthroline. The purified enzyme could completely hydrolyze a fibrin substrate within 6 h in vitro, and had a low $K_m$ value for fibrin hydrolysis. It was concluded that the purified enzyme was a metalloprotease with relatively high specificity for fibrinolysis, and thus, could be applied as an effective thrombolytic agent.

• 한국미생물·생명공학회지
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• 제18권3호
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• pp.251-259
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• 1990

생전분 분해력이 강력한 glucoamylase를 생산하는 균주로서 Asp.usamii IAM 2185를 선정하였다. 밀기울배지에서의 효소생산의 최적 initial pH는 6.0-8.0, 최적 배양온도는 25-$30^{\circ}C$, 최적 배양시간은 72시간이고, 밀기울배지에 ammonuim nitrate와 albumin의 첨가는 효소의 생산을 약간 증가시켰다. 황산암모늄분획, CM-cellulose와 DEAE-cellulose column chromatography에 의하여 효소를 정제하였고, 정제효소의 specific activity는 34.3U/mg.protein, 수율은 10.3 이었다.