• The Korean Journal of Food And Nutrition
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• v.31 no.6
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• pp.811-820
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• 2018

This study suggests a method of making cheese using soybeans for healthy food for people that are allergic to animal proteins, vegetarians, people on a diet, infants and toddlers. Additionally, the study was conducted to provide basic data that can contribute to the development of a quality control class of Korean cheese and underdeveloped cheese industry. Soybean cheeses have a high protein content and low fat. The free amino acids of soybean cheeses contained 11.48 mg of arginine per 100 g, 9.33 mg of glutamate, and leucine 4.91 mg, in that order. The free amino acids of Company A's milk cheese contained 20.95 mg of glutamate, 8.95 mg of proline and 8.02 mg of lysine per 100 g. In soybean cheeses, there were 2.21 mg of tryptophan and 0.73 mg of cysteine, which were not analyzed in the milk cheese of company A. The contents of the constituent amino acids was 1,070.22 mg of glutamate, 467.30 mg of aspartate and 446.30 mg of leucine in 100 grams of soybean cheeses per 100 grams. The milk cheese of Company A was 1,715.97 mg of glutamate, 798.72 mg of leucine and 685.31 mg of proline. The mineral contents of the soybean cheese were 120.29 mg/100 g of calcium, 0.92 mg/100 g of iron, 0.78 mg/100 g of zinc and 0.40 mg/100 g of selenium, respectively. The contents of vitamin $B_1$ and ${\beta}$-glucan in soybean cheese were higher than that of the milk cheese in Company A at 0.08 mg/100 g and 13.73 mg/g, respectively. Therefore, it is considered that the soy cheese is excellent in nutritional aspect and will contribute to health promotion. It is also suitable for people that are allergic to animal proteins, vegetarians, people on a diet and healthy foods for infants.

• Journal of Life Science
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• v.28 no.2
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• pp.223-228
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• 2018

Lactic acid bacteria were isolated from a variety of fermented seafoods and sea creatures from the East Sea Rim, Korea and were screened for ${\gamma}-amino$ butyric acid-producing (GABA) activity. Through a 16S rRNA sequence analysis, the bacteria of interest, which were GABA-positive on the thin-layer chromatography analysis, were recognized as three isolates of Lactobacillus (Lb.) brevis and one isolate of Lactococcus (Lc.) lactis. Lb. brevis FSFL0004 and FSFL0005 were isolated from fermented anglerfish and Lb. brevis FSFL0036 was derived from salted cutlass fish. The Lc. lactis strain FGL0007 was isolated from the gut of a brown sole flounder. According to HPLC analysis, the GABA contents produced by FSFL0004, FSFL0005, FSFL0036 and FGL0007 were equivalent to $10,754.37{\mu}g/ml$, $13,082.79{\mu}g/ml$, $12,290.19{\mu}g/ml$, and $45.07{\mu}g/ml$ respectively in 1% monosodium glutamate-supplemented methionyl-tRNA synthetase (MRS) broth. The four strains were inoculated in skim milk with 1% monosodium glutamate to commercialize the strains as starter cultures for GABA-enriched dairy products, and TLC results displayed the production of ${\gamma}-amino$ butyric acid by all four strains in the adaptation media. Lc. lactis FGL0007 demonstrated the greatest GABA production ($431.42{\mu}g/ml$) by HPLC analysis. The GABA production by lactic acid bacteria strains in the skim milk demonstrated in the present study may be helpful for the production of GABA-enriched dairy products.

• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.2
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• pp.223-230
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• 2008

For the use of extracts from salmon frame as a basic material of Gomtang-like products, various methods (soaking into soybean milk, adding anchovy, and adding spices) for masking fish odor into extracts from salmon frame were examined and the food component characteristics were also compared with commercial Gomtang. According to the results of volatile basic nitrogen, transmission at 660 nm and sensory evaluation of extracts, soaking treatment, which is the soaking of salmon frame into soybean milk, was the most efficient method among the various methods for masking fish odor into extracts from salmon frame. There was no difference in the proximate composition between extracts from salmon frame soaked (FS) and unsoaked (C) into soybean milk. The FS was not detected in heavy metals, such as chromium, lead and cadmium. The taste value of FS (16.26) was higher than that of C and the major amino acids were glutamic acid and aspartic acid. Total amino acid content of FS (3.08 g/100 mL) was also higher than those of C (2.95 g/100 mL) and commercial Gomtang (1.70 g/100 mL), and the major amino acids were glycine, proline, glutamic acid and arginine. The calcium and phosphorus contents of FS/500 mL accounted for 21.7% and 18.5%, respectively, of the recommended daily allowance of mineral for adult.

• Journal of the Korean Chemical Society
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• v.9 no.4
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• pp.201-210
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• 1965

Leuconostoc mesenteroides P-60, Lactobacillus arabinosus 17-5, Streptococcus faecalis R have been successfully used for the quantitative determination of sixteen amino acids in Undaria pinnatifida (Harvey) Suringar hydrolysate by alkaline and hydrolysis for succesive two hours from two to twelve hours, by means of microbiological assay. And thiamine and riboflavin were fluorometrically determinated by thiochrome and lumiflavin in powder (80mesh) of Undaria pinnatifida (Harvey) Suringar. The results were as follows: 1) Arginine contents was the highest in hydrolysate for two hours, but longer the hydrolysis, the more content Undaria pinnatifida was decreased. 2) The adequate contents of other amino acids were obtained by hydrolysis for six hours. 3) Growth check and improve of Lactobacillus were not identified in determination by microbiological assay for Undaria pinnatifida. 4) The following values were obtained in Undaria pinnatifida hydrolysate six hours: asparatic acid 466, arginine 230, lysine 317, histidine 74, isoleucine 242, methionine 202, phenylalanine 256, proline 231, threonine 231, tyrosine 161, valine 415, glycine 302, leucine 414, glutamic acid 625, cystine (5 hrs.) 53 and tryptophan (8 hrs.) 90mg per nitrogen one gram. 5) Protein score was 81 (limiting factor was isoleucine) and essential amino acids pattern was of satisfactory results. And methionine contained was higher than FAO value or milk value. 6) Sulphur contained amino acids (methionine plus cystine) contained in Undaria pinnatifida were 225mg/N-g. That was satisfactory results. 7) Absorption spectrum of wave length were not different 1% HAc from buffer-sol. (pH 6.8) in dilution for determination of riboflavin. Both methods might be suitable. 8) Thiamine and riboflavin contained in Undaria pinnatifida were ($B_1,\;82.51{\pm}1.1){\gamma}/N-g\;and\;(B_2,\;115.29{\pm}1.5){\gamma}/N-g.$.

• Journal of Life Science
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• v.19 no.9
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• pp.1258-1264
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• 2009

In this study, effects of feeding Holstein cows with TMR feed, which includes un-dried citrus byproducts, on the nutritional components of their raw milk were investigated. Two kinds of raw milk from primipara cows and multipara cows were used for the experiment: T0 (raw milk produced by dairy cows not fed with TMR feed including citrus byproducts) and T1 (raw milk produced by dairy cows fed with TMR feed including citrus byproducts). For both primipara and multipara cows, there was no statistically meaningful difference between T0 and T1 in terms of moisture, crude protein, crude fat, crude ash contents or caloric content. T1 showed a lower amount of cholesterol in raw milk for both primipara and multipara cows, which was especially statistically meaningful in multipara cows (p<0.05). Regarding mineral contents in raw milk, T1 showed significantly higher amounts of Na and S in primipara cows, and Na, Cu, Fe, S in multipara cows, respectively. For both primipara and multipara cows, there were no statistically meaningful differences between T0 and T1 in terms of the total amount of amino acids in the raw milk, the composition of saturated fatty acid/unsaturated fatty acid, vitamin A, E, $B_2$ or $\beta$-carotene, while T1 showed significantly higher levels of vitamin $B_1$ in primipara cows than T0.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.5
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• pp.741-746
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• 2005

To investigate the basic information and the possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes and ACE-inhibitory peptides were separated and purified. ACE-inhibition ratios of enzymatic hydrolysates of goat's CN and various characteristics of ACE-inhibitory peptides were determined. ACE-inhibition ratios of goat's CN hydrolysates were shown the highest with 87.84% by pepsin for 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from goat's CN hydrolysates by pepsin for 48 h was confirmed the highest ACE-inhibition activity. Fraction 3 g and Fraction 3 gh from peptic hydrolysates by RP-HPLC to first and second purification were the highest in ACE-inhibition activity, respectively. The most abundant amino acid was leucine (18.83%) in Fraction 3 gh of ACE-inhibitory peptides after second purification. Amino acid sequence analysis of Fraction 3 gh of ACE-inhibitory peptides was shown that the Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr and Tyr-Leu. IC$_{50}$ calibrated in peptic hydrolysates at 48 h, Fraction 3, Fraction 3 g and Fraction 3 gh from goat's CN hydrolysates by pepsin for 48 h were 29.89, 3.07, 1.85 and 0.87 g/ml, respectively. Based on the results of this experiment, goat's CN hydrolysates by pepsin were shown to have ACE-inhibitory activity.

• Journal of Animal Science and Technology
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• v.47 no.1
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• pp.83-90
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• 2005

ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat's whey hydrolysates was 85.5 % by pepsin for 72 hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72 hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(I 8.54 %) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-GlyVal- Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. $IC_{50}$ calibrated in peptic hydrolysates(72 hrs), F-4, F-4e and F-4ed from goat's whey hydrolysates by pepsin for 72 hrs were 33.93, 28.75, 11.74 and 1.09 mg/ml, respectively. From the results of this experiment, goat's whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.

• Food Science of Animal Resources
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• v.36 no.4
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• pp.487-493
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• 2016

The antimicrobial activity of bovine lactoferrin hydrolysates (bLFH) was measured against Pseudomonas strains (P. syringae and P. fluorescens) in vitro. To compare susceptibility to bLFH, minimal inhibitory concentration (MIC) values were determined using chemiluminescence assays and paper disc plate assays. Antimicrobial effect against P. fluorescens was not observed by either assay, suggesting that bLFH did not exhibit antimicrobial activity against P. fluorescens. However, a significant inhibition of P. syringae growth was observed in the presence of bLFH. The addition of bLFH in liquid or solid medium inhibited growth of P. syringae in a dose-dependent manner. Furthermore, a bLFH peptide with antimicrobial activity toward P. syringae was isolated and identified. The N-terminal amino acid sequences of thus obtained antimicrobial bLFH peptides were analyzed by a protein sequencer and were found to be Leu-Arg-Ile-Pro-Ser-Lys-Val-Asp-Ser-Ala and Phe-Lys-Cys-Arg-Arg-Trp-Gln-Trp-Arg-Met. The latter peptide sequence is known to be characteristic of lactoferricin. Therefore, in the present study, we identified a new antimicrobial peptide against P. syringae, present within the N-terminus and possessing the amino acid sequence of Leu-Arg-Ile-Pro-Ser-Lys-Val-Asp-Ser-Ala.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.6
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• pp.1116-1121
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• 1997

Effects of gamma irradiation onf the activity and the properties(amino acid compositions, in vitro digestibility and SDS-PAGE pattern) of proteolytic enzymes were investigated. The proteolytic activity of soluble human serine protease, enzyme in kiwi and pineapple decreased 10% and 30~65% by 5 kGy and 30 kGy, respectively. In dried pancreatin and lysozyme, the proteolytic and antimicrobial activities decreased 6~14% and 10~20% by 5kGy and 40kGy, respectively. The analysis of above 10kGy-irradiated soluble human serine protease by SDS-PAGE revealed radiolysis of the enzyme into protein or peptides of lower molecular weights. The irradiation of skim milk, hammastein casein, and lysozyme up to 40kGy had no deleterious effect on either the in vitro digestibility or amino acid compositions.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.3
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• pp.289-300
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• 1997

Newborn dog chymosin was extracted from the stomachs of dogs of 2 weeks of age, and was purified by ion exchange chromatography. Half of the sequence was determined by amino acid sequencing and the complete sequence was deduced from a cloned chymosin cDNA Results showed that the zymogen showed 79% sequence identity with calf prochymosin and 54% identity with porcine pepsinogen A The size of the propart and location of the residue which becomes the amino-terminus in the active enzyme was the same in the prochymosins. The maximum general proteolytic activity at pH 3.2 of newborn dog chymosin was 3-4% of that of porcine pepsin A at pH 2, whereas the milk clotting activity relative to the general proteolytic activity of newborn dog chymosin was much higher than that of calf chymosin. Agar gel electrophoresis at pH 5.2 of stomach extracts of individual dogs showed the existence of two predominant genetic variants of zymogen and enzyme. The two variants could not be distinguished by amino acid composition or amino-terminal sequencing, and no differences in the enzymatic properties of the genetic variants were observed. It was concluded that of the residues that participate in the substrate binding, calf and newborn dog chymosin differ in the following positions (porcine pepsin numbering, subsites in parentheses) : Ser 12 Thr(S$_4$), Leu 30 Val(S$_1$/S$_3$), His 74 Gln(S'$_2$), Val 111 Ile(S$_1$/S$_3$), Lys 220 Met(S$_4$). With regard to the low general proteolytic activity of newborn dog chymosin, the substitution Asp303 Val relative to calf chymosin may contribute to an explanation of this.