• 한국의류학회지
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• 제10권3호
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• pp.1-8
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• 1986

The purpose of this study was to investigate the characteristics of human epidermal stratum corneum as protein model soils for detergency test. The stratum corneum was collected by scraping of the skin and purified with solvent. The results obtained were as follows: 1. Purified stratum corneum contained $92.38\%$ of crude protein. 2. In the amino acid compositions, contents of glycine, glutamic acid and serine were high and methionine and cystine were low. They were similar to fibrous $\alpha$-keratin consisted of stratum corneum. Whereas the content of polar amino acids was decreased, that of nonpolar amino acids was increased after enzyme hydrolysis. 3. The hydrolysis of stratum corneum with enzyme increased muck at initial reaction time and levelled off in 4$\~$6 hours. The hydrolysis with enzyme was improved effectively at its optimum temperature and pH. 4. The hydrolysis of stratum corneum with enzyme increased by the addition of surfactants. The order of compatibility with enzyme was in the order of Triton X-100>AOS>LAS.

• 한국응용과학기술학회지
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• 제33권1호
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• pp.176-185
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• 2016

연산오계는 오래전부터 건강기능 증진 및 치료 효능이 높은 것으로 알려져 왔다. 최근 건강기능식품 소재로 기능성 펩타이드 효능이 알려짐에 따라, 연산오계 다리육으로부 올리고 펩타이드 최적 생산 공정 및 생성물 특성에 대하여 연구를 수행하였다. 최적 효소가수 분해 공정 표면반응 분석을 이용하여 수행하였다. 최적 공정 조건을 확립하기 위해서 온도 (40, 50, $60^{\circ}C$), pH (pH 6.0, 7.0, 8.0), 효소 (1, 2, 3%) 범위에서 수행을 하였다. 생성물에 대한 가수분해도, 유리아미노산, 분자량 분포를 분석하였다. 효소 가수분해 최적 온도는 $58^{\circ}C$, pH 7.5, 효소의 농도는 3% 이었다. 최적 조건에서 2 시간 효소 가수분해를 한 결과 75-80% 이었다. 유리 아미노산 총량은 168.131 mg/100 g 이었다. 분자량를 MALDI-TOF 으로 분석을 한 결과 90% 이상이 300-1,000 Da 분포를 보여주었다.

• Journal of Microbiology and Biotechnology
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• 제2권3호
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• pp.197-203
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• 1992

Studies of the pretreatment of chitin and its subsequent hydrolysis by Aspergillus carneus chitinase are reported. Ball milling was found to be the most effective way among the pretreatment methods tested. Data are presented describing the effect of enzyme and substrate concentrations on the rate and extent of the hydrolysis process. It was found that the successive addition of enzyme improved the saccharification yield. Significant product inhibition of the chitinase was observed when N-acetylglucosamine concentration was 3.6％ or higher. Adsorption of enzymes to the substrate occurred during a 24 hr hydrolysis period. An initial rapid and extensive adsorption occurred, followed by gradual desorption which increased during the time of reaction. Intermediate removal of the hydrolyzate and continuation of the hydrolysis by adsorbed enzyme on the residual chitin was also investigated. A total of 75.4 g/l reducing sugars, corresponding to 69.2％ saccharificaton yield (as N-acetylglucosamine) was obtained. In addition an increase in the amount of recoverable enzymes was observed under these conditions. Evidence presented here suggests that the technique, whereby the free enzymes in the recovered hydrolyzate are re-adsorbed onto the new substrate, may provide a means of recirculating the dissolved enzymes.

• KSBB Journal
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• 제30권2호
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• pp.53-57
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• 2015

In this study, the production of total reducing sugar from macro green-algae Enteromorpha intestinalis by enzymatic hydrolysis was investigated. As a result of enzymatic hydrolysis using 13 kind commercial enzymes, the highest yield of 8.75% was obtained from Viscozyme L, which is multi-enzyme complex such as cellulase, arabanase, beta-glucanase, hemicellulase and xylanase. As a control, only 0.33% and 0.27% yield were obtained from 1% sulfuric acid and 0.05 M citrate buffer (pH 4.8), respectively. In the case of enzyme mixture, the mixture of $Viscozyme^{(R)}$ L and $Cellic^{(R)}$ CTec2 (1:1) was presented the highest yield of 10.67%. Finally, the 14.99% yield was obtained at 36 hr under the condition of 10% biomass and 30% enzyme mixture.

• Journal of Microbiology
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• 제37권2호
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• pp.80-85
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• 1999

The purification system of glucoamylase (glucan 1,4-${\alpha}$-glucosidase, EC 3. 2. 1. 3), some characteristics of the purified enzyme and hydrolysis rate of various raw starch were investigated through several experiments. The enzyme was produced on a solid, uncooked wheat bran medium of Aspergillus oryzae NR 3-6 isolated from traditional Korean Nuruk. The enzyme was homogeneously purified 6.8-fold with an overall yield of 28.3% by the criteria of disc- and SDS-polyacrylamide gel electrophoresis. The molecular weight was estimated to be 48 kDa by SDS-PAGE. The optimum temperature and pH were 55$^{\circ}C$ and 4.0, respectively. The enzyme was stable at a pH range of 3.0∼10.0 and below 45$^{\circ}C$. Enzyme activity was inhibited about 27% by 1mM Hg2+. The hydrolysis rate of raw wheat starch was shown to be 17.5-fold faster than the hydrolysis rate of soluble starch. The purified enzyme was identified as glucoamylase because the product of soluble starch by the purified enzyme was mainly glucose by thin layer chromatography.

• Biotechnology and Bioprocess Engineering:BBE
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• 제7권2호
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• pp.57-66
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• 2002

This review focuses on the use of immobilized lipase technology for the hydrolysis of oils. The importance of lipase catalyzed fat splitting process, the various immobilization procedures, kinetics, deactivation kinetics, New immobilized lipases for chiral resolution, reactor configurations, and process considerations are all reviewed and discussed.

• 한국식품영양학회지
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• 제9권2호
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• pp.167-175
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• 1996

This studies were conducted to select optimal enzyme that produced hydrolysate from soybean, and to evaluated functionality of hydrolysate. Soybean powder was suspended with water and hydrolyzed by seven commercial proteases. Hydrolysate produced with protease from Bacillus subtilis showed the highest inhibition effect on the activity of angiotension converting enzyme(ACE), and the condition of enzymatic hydrolysis was 5cA substrate concentration, 0. l% enzyme concentration, 4 hour hydrolysis time. Under above optimum condition, soybean was hydrolyzed with protease from Bacillus subtilis yielding a DH (degree of hydrolysis) of about 49%. Hyrophobicity of hydrolysate was not correlated with the inhibition effect on ACE activity. The functionality of hydrolysate was significantly influenced by pH. Solubility of hydrolysate at alkali solution was greater than that at acidic solution.

• Journal of Pharmaceutical Investigation
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• 제21권4호
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• pp.231-236
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• 1991

The molecular nature of aspirin hydrolysis was studied using cyclodextrin as a biomimetic model for esterase. Cyclodextrin was selected for this purpose because it meets the necessary requirements for the hydrolysis study, Dissociation constants and catalytic rates were obtained under alkaline conditions by the kinetic method.

• Food Science and Biotechnology
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• 제17권4호
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

• Macromolecular Research
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• 제10권2호
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• pp.122-126
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• 2002

A molecularly imprinted polymer (MIP) having both amidine and imidazole functional groups in the active site has been prepared using p-nitrophenyl phosphate as a transition state analogue (TSA). The imprinted polymer MIP with amidine and imidazole found to have the highest hydrolysis activity compared with other MIPs with either amidine or imidazole groups only. It is postulated a cooperative effect between amidine and imidazole in the hydrolysis of p-nitrophenyl methyl carbonate (NPMC) as a substrate when both groups were arranged in proximity by molecular imprinting. The rate enhancement of the hydrolysis by MIP was 60 folds over the uncatalyzed solution reaction and two folds compared with the control non-imprinted polymer CPI having both functional groups. The enzyme-mimetic catalytic hydrolysis of p-nitrophenyl acetate by MIP was evaluated in buffer at pH 7.0 with $K_{m}$ of 1.06 mM and $k_{cat}$ of 0.137 $h^{-1}$ . . .