• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.5
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• pp.426-433
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• 2009

Fish scales have potential in functional food preparation due to their antioxidant and antihypertensive properties. We investigated the angiotensin I converting enzyme (ACE) inhibitory activity of Tilapia mossambica scale extracts. Hydrolysates of tilapia scales were prepared by enzymatic extraction using five proteases (${\alpha}$-chymotrypsin, Alcalase, Kojizyme, Protamex and trypsin) after scales were treated with hot water for 3 hr. Scale enzymatic hydrolysates prepared using both hot water and enzyme treatments exhibited elevated hydrolysis (about 25%-55%) compared to only enzyme treatment (about 15%-45%). Enzymatic hydrolysates (1 mg/mL) prepared by both hot water and enzyme treatments also showed significantly increased ACE inhibitory activities from about 20%-75%. The pattern of ACE inhibitory activities was similar to the degree of hydrolysis. Alcalase and ${\alpha}$-chymotrypsin hydrolysates displayed the highest ACE inhibitory activities ($IC_{50}$ = 0.83 mg/mL and 0.68 mg/mL, respectively). In addition, the ACE inhibitory effects of $IC_{50}$-chymotrypsin hydrolysates increased with decreasing molecular weight (5 kDa>, 10 kDa> and 30 kDa>), with the 5 kDa> fraction displaying the highest ACE inhibitory activity (about 89.9% and $IC_{50}$ = 0.1 mg/mL). We suggest that the peptide compounds of enzymatic hydrolysates prepared from tilapia scale enhances ACE inhibitory activity and might be useful as an antihypertensive material.

• Journal of the Korean Society of Tobacco Science
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• v.2 no.1
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• pp.1-7
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• 1980

Gel filtration column chromatography (Sephadex G-75), dialysis an d Brushite column chromatography were carried out to separate the brown pigmented macromolecule from water extracts of the cured leaf tobaccos. The two distinct macromolecules having different molecular weight were separated by the Sephadex column chromatography. Brushite also separated two different species of macromolecules which might have different electronic structures. According to the enzymatic degradation of protein in Burley and Hicks, chymotrypsin showed the best degradation ratio, ie., 16-30% in Burley and 38-57% in Hicks. Similar effect was observed with pepsin. However, very low effect of degradation was revealed with trypsin. The sample treated with the proteolytic enzymes revealed the disappearance of the first peak and the slight decrease of the 2nd peak height in the separation profile of Sephadex. After dialysis, the brown pigmented macromolecule was pyrolyzed at $300^{\circ}C$ and the strongly fluorescent components not identified before pyrolysis were detected with TLC separation. Absorption spectrum of these fluorescent compounds was monitored in benzene and the absorption maxima at 265nm and 275 nm were obtained. Considering absorption maxima and shape of the spectrum, those fluorescent compounds seem to be PAH derivatives.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.2
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• pp.323-329
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• 1995

For the effective utilization of dark meat separated as by-product from skip-jack canning, the dark meat concentrate(DPC) was prepared by removal of extractable materials with ethanol from dried dark meat. Dark meat protein hydrolysate(DPH) was prepared by the hydrolysis of DPC with ${\alpha}-chymotrypsin$. ${\alpha}-Chymotrypsin$ hydrolysed DPC to the extend of 79% during 10hr. The solubility over a pH range 1~12 showed similar trend on the both of DPH and DPC. The highest solubility was 81% on the DPH and was 36% on the DPC at pH 3. The lowest solubility was 65% on the DPH and was 22% on the DPC at pH 7. The content of total free amino acid was higher in the DPC than in the DPH, but the content of total essential free amino acid was higher in the DPH. Especially, the contents of taurine in the DPC and DPH were much higher than those of other amino acids. The result of sensory evaluation on the fish sauce analogue showed good taste, color and odor at the supplemented level of 8g DPH per 100ml of raw solution of fish sauce analogue and didn't show signifcaint difference compared with market fish sauce(p<0.05). On the preparation of surimi gel, 2% substitution of DPH for the supplemented starch was the most appropriate level.

• Applied Biological Chemistry
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• v.13 no.1
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• pp.65-72
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• 1970

Two peptides (Im pr-M, Im ch-M) derived from Im ${\lambda}-type$ of Bence Jones Protein and one peptide (Ikch-M) from Ik were separated and purified using the Dowex $50{\times}2$ column $(1{\times}20\;cm)$ and Dowex $1{\times}2(0.9{\times}50\;cm)$. The buffer solution was composed of 1% pyridine and IM formic acid in Dowex $1{\times}2$ column. The blocked N-terminal was examined with ninhydrin reaction before and after alkaline hydrolysis, which was fractionated by Dowex $1{\times}2$ column. Pyrro-glutamic acid in N-terminal residue was identified by comparing with the authentic pyrro-glutamic acid through a high voltage electrophoresis (pH 3.5, 3000 V.) after the peptide Im pr-M (PCA. Ser) was cleavaged at the position of serine with cone. (12 N) HCl and the pyrro-glutamic acid was converted to glutamic acid by treating it with N-NaOH for 116 hours at $27^{\circ}C$. The substractive method was applied to find out the sequence of peptides and carboxypeptidase A was employed to release C-terminal residue from the peptide. In present study PCA. Ser in Im Pr-M was isolated from the pronase digested ${\lambda}$-type Bence Jones protein. The yield of the Im Pr-M was 79.6 percent of its theoretical value, based on the molecular weight of Bence Jones Protein. Im ch-M (PCA. Ser Val. Leu) was isolated from the chymotrypsin digested ${\lambda}$-type Bence Jones Protein. The yield of the Im ch-M was 72.2 percent. based on the molecular weight of Bence Jones Protein. Ik ch-M (PCA. Ser. Ala. Leu) was isolated from the chymotrypsin digested ${\lambda}$-type Bence Jones Protein and its yield was 42% based on the molecular weight of Bence Jones Protein.

• Korean Journal of Food Science and Technology
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• v.27 no.6
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• pp.866-870
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• 1995

This study was conducted to determine the effect of soluble polysaccharides and indigestible polysaccharides on the digestibility of casein in vitro and the structure of polysaccharide. The digestibility of casein by trypsin in vitro was reduced to $80{\sim}89%$ and $69{\sim}99%$ by high molecular soluble polysaccharide (HMS-P) and low molecular insoluble polysaccharide (LMI-P) prepared from buckwheat, respectively. The digestibility of casein by chymotrypsin was reduced to $63{\sim}88%$ and$71{\sim}79%$ by HMS-P and LMI-P, respectively. But casein digestibiliy by trypsin and chymotrypsin was slightly reduced by LMS-P. The casein hydrolyzates inhibited by HMS-P gave a main peak in the void volume on Sepadex G-100, but the peak in the total volume was only appeared in case of LMS-P having no inhibito교 effect. It was suggested that the HMS-P was consisted of 4-linked and 4,6-dissubstituted glucose from the structural analysis by GC.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.20 no.6
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• pp.582-590
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• 1987

Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper. L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. The structural changes of freeze-dried filefish meat, peptic hydrolysate, FPC and plasteins were observed by Scanning Electron Microscopy(SEM). The functional properties of plasteins also were measured. The solubility of plasteins was higher than that of FPC and the Glu-plastein had $95\%$ solubility in the range of pH 3-10. The dispersibility of Glu-plastein and protease plastein was similar to that of egg albumin, but those of the other plasteins were lower. The water holding capacity of plasteins was lower than that of egg albumin and C. Lipid absorption of Leu-plastein was tile highest, holding 1.80 ml/g, and that of the other plasteins was similar to that of egg albumin. The emulsifying activity of Leu-plastein was the highest, holding $61.2\%$, and that of Glu-plastein was the lowest, holding $50.7\%$. The emulsifying stability of plasteins was similar to that of the emulsifying activity. The emulsifying capacity of Leu-plastein was 384 ml/g(the highest), but that of Glu-plastein and $\alpha-chymotrypsin$ plastein was 248 ml/g(the lowest). The Leu-plastein shelved the highest foaming capacity, $373\%$. The foaming capacity of other plasteins was higher than that of egg albumin. The foaming stability of plasteins was superior to that of egg albumin. The viscosity of plasteins was lower than that of egg albumin. The microstructure of $\alpha-chymotrypsin$ plastein by SEM wassimilar to that of papain plastein, but other plasteins showed differences in their microstructure. The microstructure of Glu-plastein had a smooth shape.

• Animal Bioscience
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• v.34 no.6
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• pp.1049-1060
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• 2021

Objective: This study assessed the effect of different levels of xylanase, β-glucanase and phytase on intestinal enzyme activities and tibia bone development in broiler chickens fed wheat-based diets. Methods: Twelve experimental diets were formulated using a 3×2×2 factorial design (three doses of phytase and two doses of both xylanase and β-glucanase) and offered to 648 day-old Ross 308 male chicks having 6 replicates groups with 9 birds per replicate and lasted for 35 days. Results: An interaction between the enzymes products improved (p<0.01) the activity of chymotrypsin. Protein content at d 10 was highest (p<0.001) with addition of phytase while general proteolytic activity (GPA) (p<0.02) and lipase activity (p<0.001) were decreased. At d 24, there were improvements in protein content (p<0.01) and lipase (p<0.04) with supplementation of superdose phytase. Addition of superdose phytase decreased in chymotrypsin (p<0.02), trypsin (p<0.01) and GPA (p<0.001). The optimum dose of xylanase decreased the chymotrypsin activity (p = 0.05), while the GPA (p<0.001) was increased with the optimum level of β-glucanase. Superdose phytase supplementation at d 10 improved maltase (p = 0.05), sucrase (p<0.001) and alkaline phosphatase (p<0.001) activities in the jejunum while aminopeptidase activity was highest (p<0.005) with the low level of phytase. Protein content of jejunum mucosa was bigger (p<0.001) in birds fed superdose phytase while maltase activity (p<0.001) at d 24 was reduced by this treatment. Sucrase (p<0.04) and aminopeptidase activities (p<0.001) improved when diets supplemented with low levels of phytase. Tibia bone breaking strength was highest (p<0.04) with addition of low level of superdose phytase or optimum level of β-glucanase. Bone dry matter content decreased (p<0.04) when diets supplemented with phytase. Conclusion: From the results obtained in this study, supplementation of superdose phytase was the most effective, however, the cost-benefit analysis of the use of such a dose needs to be evaluated.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.334-334
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• 2005

• Proceedings of the Korean Society of Crop Science Conference
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• 2017.10a
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• pp.251-251
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• 2017

• Food Science and Biotechnology
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• v.17 no.2
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• pp.279-286
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• 2008

The antioxidative activity of various enzymatic extracts from leaves of Perilla frutescens var. japonica was evaluated by measuring 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl, and alkyl radical scavenging activity using an electron spin resonance (ESR) spectrometer. For this study, the leaves were enzymatically hydrolyzed by 8 carbohydrases (Dextrozyme, AMG, Promozyme, Maltogenase, Termamyl, Viscozyme, Celluclast, and BAN) and 9 proteases [Flavourzyme, Neutrase, Protamex, Alcalase, PP-trypsin (trypsin from porcine pancreas), papain, pepsin, $\alpha$-chymotrypsin, and BP-trypsin (trypsin from bovine pancreas)]. The DPPH radical scavenging activities of Promozyme and Alcalase extracts were the highest, and the $IC_{50}$ values were 77.25 and $109.66\;{\mu}g/mL$, respectively. All enzymatic extracts of the leaves scavenged hydroxyl radical, and the $IC_{50}$ values of Celluclast and pepsin extracts which were the highest activity were 243.34 and $241.86\;{\mu}g/mL$, respectively. The BAN and $\alpha$-chymotrypsin extracts showed the highest scavenging activities, and the $IC_{50}$ values were 21.13 and $33.23\;{\mu}g/mL$, respectively. The pepsin extracts from the leaves showed protective effect on $H_2O_2$-induced DNA damage. In addition, the pepsin extracts decreased cell death in PC-12 cells against $H_2O_2$-induced oxidative damage. The findings of the present study suggest that enzymatic extracts of the leaves possess antioxidative activity.