• Journal of the Korean Society of Food Science and Nutrition
• /
• v.40 no.1
• /
• pp.89-93
• /
• 2011

This study was conducted to investigate the proteolysis and extraction conditions of deer antler for application of food materials. ProteAX (A) was the most effective enzyme for proteolysis of deer antler and the proteolysis condition was 0.5% (w/w) for enzyme concentration and 5 hr for proteolysis time. The effect of mixing enzyme ProteAX (A)+KFEN 2 (C) treatment in $60^{\circ}C$, 5 hr was investigated; soluble solid and protein content were the highest with A 0.5% (w/w) and B 0.5% (w/w) concentration. Result for DAH (deer antler hydrolysate) and DA (deer antler) prepared with extraction in $95^{\circ}C$ atmospheric pressure (AP, 6~18 hr) and extraction under $120^{\circ}C$ pressure condition (UP, 15~60 min) after hydrolysis on preceding established condition descriptions indicated that difference in pH according to enzyme treatment and extraction conditions was not significant. Sugar content of DA was $1.5^{\circ}Brix$, DA-UP (under pressure) and DAH-AP (atmospheric pressure) were $2.2^{\circ}Brix$; the highest sugar content of $2.7^{\circ}Brix$ was observed in DAH-UP for 60 min extraction. Also total free sugar, crude protein and collagen content were the highest in DAH-UP for 60 min recording at 1.97%, 742.7 mg/100 g and 498.8 mg/100 g, respectively. From these results, deer antler hydrolysate prepared with extraction under pressure was the most effective for functional characteristics enhancement. Hereafter, various practical uses of materials with enhanced characteristics of antler is expected.

• Food Science and Preservation
• /
• v.30 no.1
• /
• pp.146-154
• /
• 2023

To develop a multi-functional ingredient, the bioconversion of katsuobushi protein was optimized using Bacillus subtilis HA and Lactobacillus plantarum KS2020. The Dendropanax morbiferus extract (DME) culture with protease activity (102 unit/mL) was prepared by B. subtilis with 2% glucose and 1% skim milk through one day of alkaline fermentation. Katsuobushi protein was effectively hydrolyzed by the DME culture at 60℃ for 3 hours, resulting in a tyrosine content of 156.85 mg%. Subsequently, a second lactic acid fermentation was carried out with 10% monosodium glutamate (MSG) using L. plantarum KS2020 to produce higher levels of GABA. Following co-cultivation for three days, DME exhibited a pH of 8.3 (0% acidity). After seven days, the viable cell count of L. plantarum increased to 9.33 CFU/mL, but viable Bacillus cells were not detected. Taken together, a multi-functional ingredient with enriched GABA, peptides, probiotics, and umami flavor was developed through lactic acid fermentation using hydrolyzed katsuobushi protein. These results indicate that katsuobushi protein could be used as a byproduct to produce a palatable protein hydrolysate using alkaline-fermented DME culture as a proteolytic enzyme source.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.45 no.6
• /
• pp.545-552
• /
• 2012

This study developed a natural seasoning (NS) and characterized its food components. Hydrolysate from Alaska Pollock Theragra chalcogramma heads and sea tangle Laminaria japonica byproduct were obtained by incubating them with Neutrase for 4 h. NS was prepared by mixing sorbitol 2%, salt 2%, ginger powder 0.04%, garlic powder 0.2%, onion powder 0.2% and inosine monophosphate (IMP) 0.1% based on concentrated hydrolysates from Alaska pollock head and sea tangle byproduct before vaccum filtering. The proximate composition of NS was 82.7% moisture, 9.0% crude protein, and 5.1% ash. It had a higher crude protein content than commercial anchovy sauce (CS), it was lower in moisture and ash. The 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity and angiotensin-I converting enzyme (ACE) inhibiting activity of NS were 90.1% and 88.9%, respectively, which were superior to those of CS. The free amino acid content and total taste value of NS were 1,626.0 mg/100 mL and 165.86, respectively, which were higher than those of CS. According to the results of taste value, the major free amino acids were glutamic acid and aspartic acid. In the sensory evaluation, the color and taste of NS were superior to those of CS. No difference in fish odor between NS and CS was found.

• Journal of Dairy Science and Biotechnology
• /
• v.21 no.2
• /
• pp.97-104
• /
• 2003

It is extremely important to destroy the antigenicity of milk proteins for dietetic treatment of infants with milk allergy. Enzymatic digestion of milk protein is not only effective for destroying antigenicity, but it also is less liable to alter the nutritive value. Bovine casein was hydrolyzed with eight different commercial proteases derived from bacterias or fungi, either individually or in combination to eliminate protein allergenicity. The average molecular weight of casein hyrdolysates determined by size exclusion chromatography is about 550${\sim}$2,300 dalton range. Antigenicity of the casein hyrdolysates was not detected by heterologous passive cutaneous anaphylaxis in guinea pig-rabbit antiserum system. The inhibition test on the enzyme-linked immunosorbent assay(ELISA) showed that the antigenicity of casein hydrolysates is lowed up to 1/8,000 than that of intact bovine casein. As the enzyme reaction was carried out by the combination of bacterial and fungal protease, casein hydrolysates showed much lower bitterness and antigenicity. It suggests that these hydrolysates will be applied to many kinds of foods including the development of hypo-allergenic infant formula.

• Journal of Microbiology and Biotechnology
• /
• v.31 no.8
• /
• pp.1163-1174
• /
• 2021

Casein-derived antioxidant peptides by using microbial proteases have gained increasing attention. Combination of two microbial proteases, Protin SD-NY10 and Protease A "Amano" 2SD, was employed to hydrolyze casein to obtain potential antioxidant peptides that were identified by LC-MS/MS, chemically synthesized and characterized in a oxidatively damaged HepG2 cell model. Four peptides, YQLD, FSDIPNPIGSEN, FSDIPNPIGSE, YFYP were found to possess high 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging ability. Evaluation with HepG2 cells showed that the 4 peptides at low concentrations (< 1.0 mg/ml) protected the cells against oxidative damage. The 4 peptides exhibited different levels of antioxidant activity by stimulating mRNA and protein expression of the antioxidant enzymes such as superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px), as well as nuclear factor erythroid-2-related factor 2 (Nrf2), but decreasing the mRNA expression of Kelch-like ECH-associated protein 1 (Keap1). Furthermore, these peptides decreased production of reactive oxygen species (ROS) and malondialdehyde (MDA), but increased glutathione (GSH) production in HepG2 cells. Therefore, the 4 casein-derived peptides obtained by using microbial proteases exhibited different antioxidant activity by activating the Keap1-Nrf2 signaling pathway, and they could serve as potential antioxidant agents in functional foods or pharmaceutic preparation.

• Korean Journal of Food Science and Technology
• /
• v.26 no.4
• /
• pp.436-441
• /
• 1994

To investigate the lowering effects of in vitro enzymatic hydrolysis by the treatment of chymotrypsin, trypsin, pancreatin, or protease from Aspergillus oryzae on the antigenicity of whey protein isolate (WPI) against rabbit anti ${\alpha}-LA$ antiserum, competitive inhibition ELISA (cELISA) and passive cutaneous anaphylaxis (PCA) test using guinea pig were performed. The results of cELISA showed that the monovalent antigenicity of the whey protein hydrolysates (WPH) to the antiserum was decreased to $10^{-2.5}-10^{-5.5}$ and less by the hydrolysis. The monovalent antigenicity of the WPH hydrolyzed by trypsin, or protease from Asp. nryzae was much lowered by the pretreatment of heat denaturation. The antigenicity of the WPH hydrolyzed by chymotrypsin, trypsin, or pancreatin was much lowered by the pretreatment of pepsin. Especially, the antigenicity of TDP (trypic hydrolysate with pretreatment of heat and pepsin) was found almost to be removed. However, there was not consistency between degree of hydrolysis(DH) and the monovalent antigenicity of the WPH. By the heterologous PCA it was found that all of the PGPH lost the polyvalent antigenicity regardless of the pretreatments although WPI and ${\alpha}-LA$ had the positive high antigenicity. The results suggested that the peptides derived from ${\alpha}-LA$ in WPH could bind specific antibodies but they could not induce allergy. Therefore, it was elucidated that the allergenicity of ${\alpha}-LA$ in whey protein could be destroyed easily by the enzymatic hydrolysis.

• Korean Journal of Food Science and Technology
• /
• v.38 no.4
• /
• pp.567-570
• /
• 2006

This study was carried out to investigate the effect of antihypertensive peptides originating from marine proteins on ACE inhibitory activity and systolic blood pressure in spontaneously hypertensive rats (SHR). Sixteen male SHR (SHR/NCrj) weighing approximately 270 g were randomly divided into few experimental groups based on diet: C (control), A (anchovy), P (pollack) and M (mackerel). The final body weights of P and M groups were higher, than those of C and A groups, but difference was not significant. Average reference blood pressure (RBP) was 224 mmHg at 12 weeks old. Compared with RBP, final systolic blood pressure of the marine peptide oops after 28 days of feeding with anchovy, pollack and mackerel fractions by gavage was decreased by 9.0% (A), 10.2% (P) and 14.3% (M), respectively, but was not different in C. Especially, final blood pressure of M was lower by 32 mmHg than RBP. These results suggested that peptide originated from mackerel hydrolysate was considered to have an antihypertensive fraction as effective lowering of blood pressure in SHR.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.39 no.10
• /
• pp.1446-1451
• /
• 2010

Silk sericin protein was hydrolyzed by seven proteolytic enzymes to examine the effectiveness of the hydrolysates to bind iron. The amino acid nitrogen contents of hydrolysates by Flavourzyme were higher than the others enzymes, and its iron binding capacity showed dose-dependent increase. The bioavailability of iron binding peptide from sericin hydolysates was investigated in iron-deficient rats. Three-week-old male rats were fed iron-deficient diet for three weeks. Rats were divided into four groups (DD: no treated group on iron deficient diet, DD+HI: heme-iron treated group, DD+OI: sericin-Fe, and DD+II: inorganic iron ($FeSO_4$) treated group, and then iron supplemented by injection for one week. After oral administration for one week, the iron contents of serum and liver were significantly higher in DD+OI ($4.2\;{\mu}g/mL$ and $80.1\;{\mu}g/mL$) and DD+HI ($3.2\;{\mu}g/mL$ and $70.6\;{\mu}g/mL$) than DD ($2.0\;{\mu}g/mL$ and $47.9\;{\mu}g/mL$). Hemoglobin content of treated groups was significantly higher than DD, but the significant difference among groups was not shown. Aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels did not show any significant difference among all groups. Binding iron to peptide from sericin hydolysates seems to improve its bioavailability and to hasten the cure of iron deficiency in experimental rat.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.42 no.5
• /
• pp.417-425
• /
• 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 Environmental Science International
• /
• v.23 no.6
• /
• pp.1095-1100
• /
• 2014

Keratin wastes are generated in excess of million tons per year worldwide and biodegradation of keratin by microorganisms possessing keratinase activity can be used as an alternative tool to prevent environmental pollution. For practical use of keratinase, its physicochemical properties should be investigated in detail. In this study, we investigated characteristics of keratinase produced by Xanthomonas sp. P5 which is isolated from rhizospheric soil of soybean. The level of keratinase produced by the strain P5 increased with time and reached its maximum (10.6 U/ml) at 3 days. The production of soluble protein had the same tendency as the production of keratinase. Optimal temperature and pH of keratinase were $40^{\circ}C-45^{\circ}C$ and pH 9, respectively. The enzyme showed broad temperature and pH stabilities. Thermostability profile showed that the enzyme retained 94.6%-100% of the original activity after 1 h treatment at $10^{\circ}C-40^{\circ}C$. After treatment for 1 h at pH 6-10, 89.2%-100% of the activity was remained. At pH 11, 71.6% of the original activity was retained after 1 h treatment. Although the strain P5 did not degrade human hair, it degraded duck feather and chicken feather. These results indicate that keratinase from Xanthomonas sp. P5 could be not only used to upgrade the nutritional value of feather hydrolysate but also useful in situ biodegradation of feather.