• Journal of Life Science
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• v.22 no.2
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• pp.220-225
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• 2012

The peptides of enzymatic hydrolysates from oyster were determined by inhibitory activity against angiotensin-converting enzyme. The ACE inhibitory activity of enzymatic oyster hydrolysates increases with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex showed the best ACE inhibitory activity after 10 h. Hydrolysates were filtered through a HiSep ultrafiltration membrane (M.W. cut-off 30 kDa, 10 kDa) to obtain the peptide fractions with ACE inhibition activity. These fractions were applied to an HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$)). Six active fractions were collected and the range of ACE inhibition was from 29.56 to 85.85%. Peptide was purified from fraction B, showing the highest ACE inhibitory activity, and its sequence was Leu-Gln-Pro. These results suggest that PEH may be beneficial for developing antihypertensive food and drug.

• KSBB Journal
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• v.6 no.3
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• pp.309-319
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• 1991

A continuous stirred tank membrane reactor(CSTMR ) was developed and optimized for the production of cod skin gelatin hydrolyzates using endo-protease Alcalase. A experimental design methodology was used to optimize the four performance variables: enzyme concentration, substrate concentration, permeate flux and reactor volume. All four variables studied had an effect on substrate conversion, with enzyme and substrate concentrations being predominant. Conversion increased with the increase in enzyme concentration, with the decrease in substrate concentration, at high volumes and low flux. A strong interaction was observed between enzyme and substrate concentrations and smaller interactions between enzyme and flux and substrate and flux. The optimum operating conditions for the CSTMR process for an initial substrate concentration for 10% were $50^{\circ}C$, pH 8, flux 7.3ml/min, residence time 82 min, and Alcalase to substrate ratio 0.02(w/w). A gradual decay in reactor activity during 8 hrs was 2.1% conversion/hr. Enzyme leakage through the 10, 000 MWCO membrane was 16% at $50^{\circ}C$ and 12% at $35^{\circ}C$, 6hrs. However, there was no apparent correlation between enayme leakage and substrate conversion. The Km value for the CSTMR was 20 times higher than the batch reactor. The productivity(expressed as mg product/mg enzyme) of the CSTMR was more than six fold higher than the batch at $50^{\circ}C$. The hydrolyzate was non-bitter.

• Korean Journal of Food Science and Technology
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• v.12 no.1
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• pp.45-52
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• 1980

The nylon (poly 6, 10) microcapsules containing ${\beta}-galactosidase$ were obtained by the interfacial polymerization of 1, 6-diaminohexane and sebacoyl chloride with ${\beta}-galactosidase$ from Escherichia coli. They were generally spherical and had a mean diameter of $80{\mu}$ with 45 % of the activity recovery. In particular, there was no transport hamper of lactose through the membrane of microcapsules. The characteristics of the microencapsulated enzyme were similar to those of soluble enzyme optimal pHs, $7.0{\sim}7.2$ for the soluble and $7.3{\sim}7.5$ for the microencapsulated ; optimal temperatures, $50^{\circ}C$ for both ; apparent $K_m,\;3.33{\times}10^{-4}(on ONPG),$ $2.86{\times}10^{-3}$ M(on lactose) for the soluble and $5.28{\times}10^{-4}$ (on ONPG), $4.25{\times}10^{-3}$ M (on lactose) for the microencapsulated ; activation energies, 8.94 for the soluble and 9.78 Kcal/mole for the microencapsulated enzyme. Using this microencapsulated ${\beta}-galactosidase$, hydrolyses of lactose and milk lactose were carried out and 80 % of 5 % lactose solution and 70 % of lactose in skim milk were hydrolyzed in 40 hr at $27^{\circ}C$. The reusability and operational stability showed that the remaining activity was 50 % of the original activity after 5 runs and 120 hr of total operating time at $27^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.30 no.2
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• pp.245-252
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• 1998

The chitosanolytic capabilities of cellulases, glucosidases, proteases and commercial enzymes were evaluated, and effective chitosanolytic cellulases from T. viride, T. reesei and Celluclast, a commercial enzyme from T. reesei were characterized. The reaction of cellulase from T. viride, T. reesei and Celluclast was optimal at pH 5. 0 and $45{\sim}55^{\circ}C$. Max. chitosanolytic activities of cellulases from both T. viride and T. reesei were observed at the enzyme/chitosan ratio=0.1 and chitosan concentration=3.0%. For the possible application of commercial Celluclast to chitosan oligosaccharides production, 3%(w/v) chitosan was reacted with 1%(v/v) Celluclast at pH 5.0 and $55^{\circ}C$. The apparent viscosity decreased by 98% within 30 minutes reaction and Max. contents of 50% EtOH solubles were 70% at 15 hrs reaction. Total reducing sugars were also increased with reaction time and maintained approx. 13.5% after 2hrs reaction. In 15 hrs treated chitosan hydrolyzates, various kinds of chitosan oligosaccharides were produced and contents of chitosan hexamer, known for its antitumor activities, were about 8.0%, about 4 times higher values compared with acid hydrolysis method. The results suggested that chitosan oligosaccharides could be produced with low-cost cellulases from T. reesei.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.11
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• pp.1640-1646
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• 2010

The optimum condition was investigated for the extraction of glycosaminoglycan (GAG) from sea hare, Aplysia kurodai. The most effective enzyme was Flavourzyme for extraction of glycosaminoglycan. The optimum incubation temperature and time for hydrolysis were $60^{\circ}C$ and 15 hr, respectively. The yield of precipitated polysaccharide depended on Brix and ethanol volume. The most effective concentration of Brix and ethanol were sixty and 5 volume of ethanol, respectively. Most GAG was eluted between 0.5 M and 0.75 M NaCl gradient on DEAE-Sepharose column, and identified by electroconductivity. The contents of hexuronic acid from polysaccharide extract and GAG were 1.0 g/100 g and 6.0 g/100 g, respectively. Hexosamine of polysaccharide and GAG as indicator of GAG component was 5.6 g/100 g and 25.7 g/100 g, respectively. GAG was identified as heparan sulfate compared with bands of other GAG on agarose gel electrophoresis, and its molecular weight was 29.6 kDa on Superdex 200 HR column.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1994.04a
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• pp.186-186
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• 1994

Many agonists have been known to activate the hydrolysis of membrane phospholipids through the bindings with corresponding receptors on the various cells. Diacylglycerol and inositol 1,4,5-trisphosphate(IP3) generated by the action of phosphoinositide-specific phospholipase C (PI-PLC) are well known second messengers for the activation of protein kinase C and the mobilization of Ca2+ in many cells. Three types of PI-PLC isozyme (${\alpha}$,${\gamma}$, and $\delta$) and several subtrpes for each type have been identified from mammalian sources by purification of enzymes and cloning of their cDNAs. Each type PI-PLC isozyme is coupled to different receptors and mediators, for example, ${\beta}$-types are coupled to the seven-transmembrane-receptors via Gq family of G-proteins and ${\beta}$-types directly to the receptor tyrosine kinases. Specific modulators for the signaling pathway through each type of PI-PLC should be very useful as potential potential candidates for lend substances in developing novel drugs. To establish the sensitive and convenient screening systems for searching modulators on PI-PLC mediated signaling, two kinds of approaches have been tried. (1) Establishment of in vitro assay condition for each type of PI-PLC isozyme: Overexpression by using vaccinia virus and purification of each isozyme was carried out for the preparation of large amounts of enaymes. Optimum and sensitive assay condition for the measurements of PI-ELC activities were established. (2) Development of the cell lines in which each type of PI-PLC is permanently overexpressed: A fibroblast cell line (3T3${\gamma}$1-7) in which PI-PLC-${\gamma}$1 was overexpressed by using pZip-neo expression vector was developed and used for the measurement of PDGF-induced IP3 formation. The responses for IP3 formed in 3T3${\gamma}$1-7 cells by the treatment of PDGF is 8 times more sensitive than those in control cells. 3T3${\gamma}$l-7 cell is useful for the screening of the inhibitors on the PDGF-induced cellular responses from large number of samples in a small volume(50 ${\mu}$l) and short time(5-15 min). Using these systems, we screened hundreds of herb-extracts for the inhibition of PDGF-induced IP3 formation and selected several extracts that showed the inhibition as the candidates for isolation and characterization of active substances. The determination of the acting point of selected extracts or fractions in the PDGF signaling pathway has been analyzing.

• Korean Journal of Food Science and Technology
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• v.23 no.6
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• pp.732-738
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• 1991

Corsoy 79 soybeans were ground into 8-(coarse) and 24-mesh (fine) full-fat soy flours. From the particle size analysis, the 8-mesh full-fat soy flours were found to have larger values for geometric mean diameter and geometric standard deviation. However, the distribution moduli of coarse and fine soy flours were similar and indicated soybeans were nearly 'brittle'. Development of hydrolytic and oxidative rancidities of coarsely and finely ground full-fat soy flours were followed from grinding to 24 hrs later. No increases in peroxide value and conjugated dienes in the oil and hexanal content in the headspace of the flour were observed when the moisture was 10.7% or less. At 14.9% moisture and above, lipid oxidation increased with increased moisture content and storage time. Free fatty acid contents increased slightly at all moisture contents. However, hydrolysis did not exceed 0.06% over the moisture range of 4 to 18%, which is of little practical significance. Fine grinding increased oxidative and hydrolytic rancidities, especially at 14.9% moisture and above. these findings indicate that raw soybeans can be ground to full-fat soy flours and stored up to 24 hrs without undergoing significant lipid and flavor deterioration if the moisture content is 11% or less.

• Korean Journal of Food Science and Technology
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• v.41 no.5
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• pp.522-527
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• 2009

The principal objective of this study was to assess the effects of various manufacturing conditions of soy sauce containing hydrolyzed vegetable protein (HVP) (HVP-soy sauce) on 3-monochloropropane-1,2-diol (3-MCPD) contents. Various HVP soy sauces were prepared under different conditions of alkaline treatment and retention process. Derivatives of heptafluorobutylimidazole (HFBI) 3-MCPD were determined via GC/MS below $0.010{\mu}g/g$, which was sensitive with a good recovery rate. The quantity of 3-MCPD decreased with the pH and temperature of alkaline treatment, and the time and temperature of the retention process increased. Alkaline treatment at pH 10.0-10.5 and a 72 hr retention process were shown to reduce effectively the 3-MCPD contents of HVP-soy sauces. This result indicates that the manufacturing process, particularly alkaline treatment, and retention process would be critical steps in managing 3-MCPD contents in HVP-soy sauce.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.5
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• pp.417-425
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• 2009

The potential utility of fish scales to the functional food industry has been investigated due to its antioxidant and antihypertensive characteristics. In this study, we report on the reactive oxygen species (ROS) scavenging and angiotensin I converting enzyme (ACE) inhibitory activities of gelatin hydrolysates processed from Branchiostegus japonicus scales, which are also high in protein content (about 46.1%). We prepared the enzymatic gelatin hydrolysates with four proteases (${\alpha}$-chymotrypsin, Alcalase, Neutrase and trypsin) from B. japonicus scale gelatin, which was prepared according to different reaction times, substrate/enzyme ratios and substrate concentrations. The enzymatic hydrolytic degrees of the gelatin increased time-dependently up to 6 hrs, while the Alcalase gelatin hydrolysates showed the highest hydrolysis degrees compared to the others. Furthermore, gelatin hydrolysates of Neutrase and ${\alpha}$-chymotrypsin showed the highest DPPH radical and $H_2O_2$ scavenging activities ($IC_{50}$ value; 9.18 mg/mL and 9.74 mg/mL), respectively. However, the activities were not significant (P<0.05). We also observed that the four gelatin hydrolysates significantly increased ACE inhibitory activities from approximately 20% to 60% (P<0.05), Among them, the Alcalase gelatin hydrolysates showed the higher ACE inhibitory activity ($IC_{50}$ value; 0.73 mg/mL) compared to the others. These results suggest that the enzymatic gelatin hydrolysates prepared from B. japonicus scales may possess a potentially useful function as an ACE inhibitory agent. As such, the utility of B. japonicus scales should be given due consideration for application in the functional food industry.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.13 no.12
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• pp.6196-6202
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• 2012

Oligo-alginate derivatives were extracted from brown algae and its antimicroalgal effects and reaction mechanism were investigated. Oligo-alginate derivatives were produced from sequential hydrolysis of high molecular weight alginate by treatment of 2 N HCl and 1% $H_2O_2$. Antimicroalgal activity of extracts was proportional to reaction time and activity was highest at 4 hrs. When oligo-alginate derivatives were treated to Akashiwo sanguinea and Cochlodinium polykrikoides, mobilities of cells were ceased. A. sanguinea cells were crushed and plasmolysis was induced in C. polykrikoides cells. To investigate the action mechanism of oligo-alginate derivatives, changes of intracellular (pHi) and extracellular pH (pHe) were determined in the microalgal cells exposed to 0.05% of oligo-alginate derivatives. pHi was decreased about 0.3 unit and pHe was increased about 0.9 unit. These results suggested that change of membrane potential by oligo-alginate derivatives could led to microalgal cell death.