• Microbiology and Biotechnology Letters
• /
• v.27 no.5
• /
• pp.354-358
• /
• 1999

In order to know the antifungal characteristics of saturated fatty acids having 6 to 12 carbons, their minimum inhibitory concentrations (MICs) and minimum fungicidal concentrations (MFCs) were estimated against Saccharomyces cerevisiae. Fatty acids from C6 to C11 exhibited increasing activity with chain length, but C12 fatty acid did not show activity at all. In relation to antifungal modes of actions, fatty acids investigated showed on inhibitory activity toward the plasma membrane H+-ATPase of Saccharomyces cerevisiae. Their inhibitions to the glucose-induced acidification and ATP hydrolysis caused by the proton pump were found to be in common wiht antifungal activities. At the test concentration of 1mM, hexanoic acid (C6) showed the lowest inhibition of about 30%, while undecanoic acid(C11) showed the strongest inhibition of over 90%. In addition, as seen with antifungal activity, the inhibitory activity of dodecanoic acid (C12) was suddenly reduced to less than 50%.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.21 no.5
• /
• pp.513-518
• /
• 1992

Optimum conditions for enzymatic hydrolysis of purified rapeseed(Brassica napus var. Youngsan) protein were investigated. Pronase showed higher activity in the hydrolysis of rapeseed protein than that of alcalase and neutrase. Preheated treatment of the rapeseed protein decreased the activity of pronase. The degree of hydrolysis of rapeseed protein was greater in distilled water than in phosphate buffer solution. Degree of hydrolysis was reached in steady state after 1 hr. Optimum conditions of the hydrolysis of the rapeseed protein were $40^{\circ}C$ in reaction temperaturem pH 8.0 in substrate solution, 1/100 (w/w) in the ratio of enzyme to substrate and 1% (w/v) in substrate concentration for pronase, respectively. At the optimum hydrolysis conditions, Km value was 3.48% (w/v).

• The Korean Journal of Pesticide Science
• /
• v.5 no.1
• /
• pp.24-29
• /
• 2001

This study was conducted to investigate insecticidal activities of Ginkgo biloba (L.) leaves-derived bilobalide and its hydrolysis and oxidation products against adults of Nilaparavata lugens Stal. To find out active insecticidal moiety of bilobalide, decomposed intermediates and derivatives of bilobalide were made by hydrolysis, oxidation, and acetylation. The structures of hydrolysis product by base and oxidation product by acid were identified as cyclopentenone analogues and trilactone sesquiterpene from dehydration of bilobalide, respectively. Insecticidal activities of the decomposed intermediates and the derivatives of bilobalide decreased in the order of bilobalide, monoacetate, ginkgolide C, oxidation product, diacetate, and hydrolysis product. Therefore, trilactone structure of bilobalide may be essential for its insecticidal activity.

• KSBB Journal
• /
• v.20 no.2 s.91
• /
• pp.129-132
• /
• 2005

This work was a method that used an acid hydrolysis for increasing the efficacy of decreasing alcohol concentration from Hovenia dulcis extract. For acid hydrolysis, the best pH was 2.0 to obtain a maximum alcohol dehydrogenase activity at fixed reaction temperature and time. At pH 2.0, reaction temperature $80^{\circ}C$ and reaction time 4 hr gave the highest activity which was $124\%$ of control. The bioactive compound, (+)-dihydromyricetin, content increased to $30\%$ after acid hydrolysis. This is very simple and efficient method to increase the efficacy of decreasing alcohol concentration from Hovenia dulcis extract.

• Journal of Microbiology and Biotechnology
• /
• v.9 no.4
• /
• pp.514-517
• /
• 1999

Hydrolysis of EFB (empty fruit bunch) derived from oil palm was studied using crude enzyme from Aspergillus terreus IMI 282743 along with commercial enzymes from Trichoderma reesei and Aspergillus niger. Hydrolysis at $40^{\circ}C$ and $50^{\circ}C$ with $\alpha$-cellulose or EFB gave significantly lower yield when commercial enzymes of T. reesei and A. niger were used and the hydrolysis time extended beyond 10 h. After 24 h of hydrolysis at $40^{\circ}C$ and $50^{\circ}C$, the filter paper activity (Fpase) from A. terreus retained as much activity as A. niger and it was significantly higher than T. reesei. Glucose concentration of 0.25% and 0.5% caused significant inhibition in the crude enzyme, but in regards to the commercial enzymes it only showed a slight effect. Crude enzymes from A. terreus could produce the highest reducing sugars when compared to commercial enzymes from T. reesei or A. niger. Nevertheless, low yield of sugar was observed for EFB for all treatments.

• Preventive Nutrition and Food Science
• /
• v.20 no.3
• /
• pp.183-189
• /
• 2015

In the present study, an optimum protease was selected to hydrolyze the egg white liquid protein for the antioxidant peptides. Alcalase treatment yielded the highest amount of ${\alpha}$-amino groups (15.27 mg/mL), while the control (no enzymatic hydrolysis) showed the lowest amount of ${\alpha}$-amino groups (1.53 mg/mL). Alcalase also gave the highest degree of hydrolysis (DH) value (43.2%) and was more efficient for egg white liquid hydrolysis than the other enzymes. The Alcalase hydrolysate had the highest radical-scavenging activity (82.5%) at a concentration of 5.0 mg/mL. The conditions for enzymatic hydrolysis of egg white liquid with Alcalase were selected as substrate : water ratio of 2:1. Five percent Alacalse treatment did not show significant (P>0.05) increases of DH and ${\alpha}$-amino nitrogen content after 24 hhydrolysis. Thirty two hour-hydrolysis with 5% Alcalase is sufficient to make antioxidative egg white liquid hydrolysate from egg white liquid. DPPH and ABTS radical-scavenging activities were significantly (P<0.05) higher after enzymatic digestion. These results suggest that active peptides released from egg-white protein are effective radical-scavengers. Thus, this approach may be useful for the preparation of potent antioxidant products.

• Food Science of Animal Resources
• /
• v.34 no.3
• /
• pp.362-371
• /
• 2014

This study utilized commercially available proteolytic enzymes to prepare egg-white protein hydrolysates (EPHs) with different degrees of hydrolysis. The antioxidant effect and functionalities of the resultant products were then investigated. Treatment with Neutrase yielded the most ${\alpha}$-amino groups (6.52 mg/mL). Alcalase, Flavourzyme, Protamex, and Ficin showed similar degrees of ${\alpha}$-amino group liberation (3.19-3.62 mg/mL). Neutrase treatment also resulted in the highest degree of hydrolysis (23.4%). Alcalase and Ficin treatment resulted in similar degrees of hydrolysis. All hydrolysates, except for the Flavourzyme hydrolysate, had greater radical scavenging activity than the control. The Neutrase hydrolysate showed the highest 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity ($IC_{50}=3.6mg/mL$). Therefore, Neutrase was identified as the optimal enzyme for hydrolyzing egg-white protein to yield antioxidant peptides. During Neutrase hydrolysis, the reaction rate was rapid over the first 4 h, and then subsequently declined. The $IC_{50}$ value was lowest after the first hour (2.99 mg/mL). The emulsifying activity index (EAI) of EPH treated with Neutrase decreased, as the pH decreased. The EPH foaming capacity was maximal at pH 3.6, and decreased at an alkaline pH. Digestion resulted in significantly higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS radical scavenging activity. The active peptides released from egg-white protein showed antioxidative activities on ABTS and DHHP radical. Thus, this approach may be useful for the preparation of potent antioxidant products.

• Korean Journal of Food Science and Technology
• /
• v.23 no.1
• /
• pp.25-30
• /
• 1991

Chicken liver was enzymatically hydrolyzed with an alkaline protease and determined the optimal conditions of reaction temperature and time, pH and enzyme to substrate ratio(E/S ratio) for possible utilization as a protein supplementary ingredient. The functional properties of hydolysate measured were water and oil absorption capacity, emulsifying activity and viscosity and sensory properties were also evaluated. It was found that hydrolysis at $60^{\circ}C$ and pH 8.0 were most effective and the degree of hydrolysis increased with increasing E/S ratio. A decrease in water and oil absorption capacity and an increase in viscosity were found during hydrolysis. The lowest emulsifying activity and highest water absorption were measured for 1/2 hour-hydrolysate and little difference was found for those treated more than 1 hour. The sensory characteristics of odor showed no significant difference among the chicken liver hydrolysates while the brightness increased and red decreased significantly(p<0.01) as the hydrolysis proceeded.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.39 no.3
• /
• pp.269-277
• /
• 2006

This study prepared functional oyster hydrolysates using two-step enzymatic hydrolysis and investigated their functional properties. To prepare two-step enzymatic hydrolysates (TSEH), oysters were hydrolyzed using 1% Protamex (PR) at $40^{\circ}C$ and pH 6.0 for 1 hr before sequential treatment with one of the following enzymes for 1 hr: Alcalase (AL), Flavourzyme (FL), Neutrase (NE), pepsin (PE), and trypsin (TR). The PRAL, PRNE and PRTR hydrolysates had significantly greater angiotensin I converting enzyme (ACE) inhibitory activity than did PR and the other TSEHs. Only the antioxidant activity of the PRNE hydrolysate was significantly different (p<0.05), while none of the TSEHs had antimicrobial activity. The oyster hydrolysate prepared by sequential treatment with Protamex and Neutrase (PRNE) had the best ACE inhibitory activity and antioxidant activity, with $IC_{50}$ values of 0.40 and 0.94 mg/mL, respectively. The PRNE hydrolysate was processed through an ultrafiltration (UF) series with molecular weight cut-off (MWCO) membranes of 3, 5, 10, and 30 kDa, and the ACE inhibitory, antioxidant, and antimicrobial activities of the permeates were determined. The permeate through the 3-kDa MWCO membrane had greater ACE inhibitory activity and antioxidant activity than did the other PRNE permeates, with $IC_{50}$ values of 0.11 and 0.40 mg/mL, respectively.

• Food Science and Biotechnology
• /
• v.17 no.4
• /
• pp.873-877
• /
• 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.