• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.30 no.5
• /
• pp.842-849
• /
• 1997

This study was designed to investigate the antioxidative activity of enzymatic hydrolysates prepared from defatted anchor muscle by various pretenses. In these hydrolysates, the hydrolysates derived from pepsin and Protamex showed the strongest antioxidative activity. Enzymatic hydrolysates also showed the synergistic effects on antioxidative activity of $\alpha-tocopherol$, and almost no change in butylated hydroxytoluene (BHT). Peroxidation of metal ions $(Fe^{3+},\;Cu^{2+})$ was inhibited by enzymatic hydrolysates. Ten fractions (P-1 to P-10) were fractionated from the peptic hydrolysates by Amberlite IR-120 and Bio-gel P-2 column chromatography. The maximum antioxidative activity was observed in the traction P-2 (fraction No. $26\~31$). In amino acid composition of before and after hydrolysis of defatted anchovy muscle and the active fractions (P-2), contents of aspartic arid and glutamic acid were increased, but alanine, cysteine, tyrosine and phenylalanine were decreased.

• Applied Biological Chemistry
• /
• v.12
• /
• pp.75-81
• /
• 1969

In order to obtain a method of scouring of raw silk and degumming of cocoon by the appling of bacterial enzyme of sericinase, a strain of proper bacteria was isolated and some properties of the enzyme produced by the isolated bacteria were studied and the following results were obtained. 1) Optimum pH and temperature were indicating 7.5 and $50^{\circ}C$. and on these conditions, the silk fibroin will get no modification at all. 2) Sericinase activity was inhibited by calcium ion in the free incubation but same ions reacted as an activator in the reaction with substrate. So, degumming of Tussah cocoon which contains calcium oxalate in the cocoon layer will be possible by the treatment of this enzyme. 3) This bacterial sericinase never gives any affection to the fibroin layer of the silk. 4) The factors of smooth-surface condition, damage of fibroin layer, touching, luster and degumming effect of the silk resulting by the enzyme treatment were more appropriate than the results of other scouring methods, saponin, alkali and saponin-alkali using methods. We expect to get the same scouring result that compared with the papain or pancreatin were applied.

• The Korean Journal of Food And Nutrition
• /
• v.16 no.4
• /
• pp.388-396
• /
• 2003

The freeze dried young antler residue was extracted by proteases and hydrochloric acid(HCl). The young antler was extracted by water at 50$^{\circ}C$ and the residue was reacted by proteases for 5 hours at 50$^{\circ}C$. The extraction rate of its residue was 32.8%(absorbance 3.61 at 280nm) of bacteria protease, 23.8%(absorbance 0.69) of papain, and 31.2% (absorbance 2.96) of pepsin. The young antler was extracted by boiling water and the residue was reacted by proteases for 5 hours at 50$^{\circ}C$. The extraction rate of its residue was 45.0%(absorbance 3.61) of bacteria protease, 30.4%(absorbance 0.33) of papain, and 51.2% (absorbance 2.77) of pepsin. The result of HPLC analysis reveals that in 50$^{\circ}C$ water extract and boiling water extract, all high molecular peak was reduced under MW 1,000 by proteases. The result from the extract of young antler residue reacted by HCl for 5 hours at 50$^{\circ}C$ shows that its extraction rate was 45% (absorbance 0.78) in concentration of 0.1N HCl, 61% (absorbance 1.82) in 0.2N, 81% (absorbance 2.29) in 0.4N, and 82.0% (absorbance 3.28) in 2.0N. The result of HPLC analysis also reveals that in the extract by 0.8N HCl, the peak of about MW 70,000 accounted for 78% in total. Protein content of the extract by 0.8N HCl was 8.2%, and content of amino acid was 81.6%, ash was 1.3%, and mineral contents were 0.1 % of Ca, 2.3% of P, 0.8 % of Mg, 3.4% of Na, 0.002% of F by dry base.

• Microbiology and Biotechnology Letters
• /
• v.15 no.2
• /
• pp.129-134
• /
• 1987

Aspergillus sp. (MK-24) producing a biological active substance that inhibited the venom proteinase activity was isolated from soil. The substance also inhibited the activity of trypsin and coagulation of blood, but did not inhibit papain, $\alpha$-chymotrypsin and pepsin. The substance was partially purified from culture filtrate by precipitaion with acetone, and by chromatography of DEAE-Sepadex A-50 column and Amberlite IRC-50 ion exchange. The inhibitory substance was stable in the wide pH range from 2.0 to 12.0 at 37$^{\circ}C$, but not stable at $65^{\circ}C$ in the alkaline pH. Only 12% of the activity was decreased by the heat treatment at 10$0^{\circ}C$ for two hours. The inhibition on venom proteinase (Agkistrodon bromohoffi brevicaudus) was a mixed type. The inhibitory activity depended on the preincubation time and completely depressed by cupric, zinc and cobalt ions. The inhibition on the venom proteinase was appeared strongly on casein but not on ovalbumin or hemoglobin as a substrate.

• Food Science and Preservation
• /
• v.10 no.2
• /
• pp.192-199
• /
• 2003

To prepare soybean curd utilizing effectively bioactive component of soybean, ultra fine whole soybean flour(UFWSF) was used as a soybean curd material for preparation of uncompressed whole soybean flour curd(UWSFC) in this study. The UWSFC was made with treatment by proteinase and coagulant, and proximate composition, color, textural properties and sensory evaluation of that were analyzed. Protease produced from Aspergillus sojae, bromelain and papain showed soybean curd coagulation ability and the pretense produced from Aspergillus sojae showed the highest soybean curd coagulation ability. When, after first heating and homogenizing, the proteinase was added to soybean milt textural properties of UWSFC were the best. Hunter's L and b values and textural properties (hardness, fracturability springiness, gumminess and chewiness) of UWSFC using proteinase and coagulant were higher than commercial soft soybean curd and adhesiveness and cohesiveness showed contrary tendency.

• Korean Journal of Food Science and Technology
• /
• v.51 no.5
• /
• pp.473-479
• /
• 2019

Gryllus bimaculatus (GB) has recently been registered as a food variety in Korea. In the present study, we prepared protein hydrolysates from GB and evaluated their antioxidant capacity. Protein hydrolysates were prepared from dried GB using enzymatic hydrolysis using five different proteases, and protein hydrolysates showing high hydrolysis value (alcalase, flavourzyme, and neutrase) were separated further into fractions ${\leq}3kDa$ and then lyophilized. Based on $RC_{50}$ values of hydrolysates (${\leq}3kDa$) obtained from four different antioxidant analyses, the flavourzyme hydrolysates showed relatively high levels of antioxidant capacity among the three hydrolysates, and in particular, it showed considerably strong antioxidant activity in 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays. The flavourzyme hydrolysate also significantly inhibited peroxidation of linoleic acid. These results suggest that protein hydrolysates from GB represent potential sources of natural antioxidants. Our current studies are focused on identification of active peptides from the flavourzyme hydrolysate.

• Food Engineering Progress
• /
• v.22 no.4
• /
• pp.309-314
• /
• 2018

In recent years, interest in halal authentication from the domestic food and cosmetics field has been growing for advances into the overseas halal market. For halal authentication, the product must not contain haram ingredients derived from pig, dog, human, GMO, etc. In this study, the presence of haram ingredients in plant extracts (carrot, oyster mushroom, and pine needle) treated with papain and bromelain and cosmetics (mask pack and cream) containing these extracts were analyzed by PCR to confirm whether these cosmetics were suitable for halal authentication. Detection limits of the PCR method that specifically detected template DNA of human, pig, dog, and GMO were $1.29{\times}10^3$, $1.14{\times}10^3$, $1.24{\times}10^2$ and $2.02{\times}10^3copies/tube$, respectively. PCR was not inhibited by the plant extracts or cosmetic ingredients. Results of PCR for the plant extracts or cosmetics containing these extracts were all negative. This PCR method could be used to rapidly identify the presence of haram ingredients in raw materials or final products during the manufacturing process of food and cosmetics.

• Food Science of Animal Resources
• /
• v.40 no.1
• /
• pp.74-86
• /
• 2020

Horse meat is nutritionally adequate to the elderly, but it has a comparatively hard texture in contrast to most of the food. In practice, the meat intake in the elderly is generally bated because the relatively difficult texture of the meat can diminish mastication. Thus, strategies are being developed to produce meat products remanding detracted mastication exertion and possibly exalt ingestion and nutritional stand, in the elderly. Hence, the effects of enzymes on textural characteristics of horse meat were studied, because they have well-known favorable efficacy on the meat tenderness by causing important demotion of the myo-fibrillar protein and collagen. Four treatments namely, papain, bromelin, pepsin, and pancreatin, alongside one control were invoked to the horse meat. Their effects on the texture parameters were determined. All the above enzymatic treatments significantly reduced hardness and resilience (p<0.001). These results present opportunities to produce essential fatty acids fortified horse meat with soft texture and satisfied technological characteristics. The intake of the essential fatty acids intensified horse meat could aid the elderly to get their aimed essential fatty acid demands. Results also suggest that horse meat tenderized through enzymatic processing stand for auspicious options for the comprehension of texture-revised diets in the elderly population.

• Journal of Marine Bioscience and Biotechnology
• /
• v.7 no.1
• /
• pp.19-27
• /
• 2015

The objective of the current study was to evaluate the inhibitory and antioxidant activities of powdered katsuobushi (dried bonito) protein hydrolysates and their corresponding fractions. The powdered katsuobushi (dried bonito) hydrolysates were obtained by enzymatic hydrolysis using Alcalase, ${\alpha}$-chymotrypsin, Neutrase, pepsin, papain, and trypsin. The antioxidant efficacy of the respective hydrolysates were evaluated using 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, and alkyl radical-scavenging activities. Among the hydrolysates, the peptic-derived hydrolysate exhibited the highest antioxidant activity compared to other enzymatic hydrolysates. Therefore, the peptic-derived hydrolysate was further analyzed, and was found to contain an active peptide with an amino acid sequence identified as Pro-Met-Pro-Leu-Asn-Ser-Cys (756 Da). The purified peptides from powdered katsuobushi (dried bonito) had an $EC_{50}$ value of $105.82{\mu}M$, and exhibited an inhibitory effect against DNA oxidation induced by hydroxyl radicals. Taken together, these results suggests that powdered katsuobushi (dried bonito) could be used as a natural antioxidant in functional foods and prevent oxidation reactions in food processing.

• Preventive Nutrition and Food Science
• /
• v.2 no.4
• /
• pp.321-327
• /
• 1997

High Temperature-cooking conditions of cultured fishes(loach, crucian carp, bastard halibut, and jacopever) were optimized by response surface methodology(RSM), and plastein products were prepared using enzymatic hydrolysis. Four models were proposed with regard to effects of time(t), temperature(T), and water/fish meat (w/f) ratio on the amount of 0.3M TCA soluble fractions. The model coefficients were ranged from p<0.0001 for jacopever to p<0.0433 for bastared halibut. Cooking conditions for 60% hydrolysis were optimized at 1) 14$0^{\circ}C$ except for crucian carp(136$^{\circ}C$); 2) 10.08 hours(loach), 7.25 hours(crucian carp), 9.85 hours(ba-stard harlibut), and 9.37 hours(iacopever); 3) 1:1(w/f) ratio except for the crucian carp(1.1:1). When protein hydrolyzates were employed for the plastein synthesis, optimum plastein-reaction conditions were determined to be pH 9.0 with chymotrypsin for the loach and crucian carp hydrolyzates, pH 9.0 with papain for the bastard halibut hydrolyzate, and pH 11.0 with trypsin for the jacopever hydrolyzate. Plastein reaction could be performed in water at concentration up to 20%(w/f).