• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.5
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• pp.745-751
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• 2003

This study was carried out to investigate whether peptide produced from wheat protein by enzyme hydrolysis can be used as a natural antimicrobial agent. Antimicrobial peptide was obtained from wheat protein hydrolyzed by 7 of pretense. The produced antimicrobial peptide was purified through ultrafiltration, membrane filtration and HPLC and molecular weight and amino acid sequence of the purified antimicrobial peptide were determined. Among hydrolysate produced from wheat protein by 7 of protease, antimicrobial activity was observed for the peptide obtained from Asp. saito protease. The Asp. saito protease did produce antimicrobial hydrolysate showing the highest antimicrobial activity at reaction condition of 37$^{\circ}C$ and pH 6.0, but not at reaction condition above 5$0^{\circ}C$. Wheat protein hydrolysate was fractionated by membrane filtration and showed antimicrobial activity between molecular weight 1,000~3,000. The antimicrobial activity fraction obtained by membrane filtration was separated through HPLC and showed antimicrobial activity in the peak of retention time 31.1~31.8 min. We could convince this hydrolysate as heat-stable peptide since antimicrobial activity was maintained after treated with heat for 15 min at 121$^{\circ}C$. Molecular weight of antimicrobial peptide identified by MALDI-mass was 1,633. Amino acid sequence of antimicrobial peptide was cysteine, glycine, prolin, prolin, prolin, valine, valine, alanine, alanine and arginine.

• Korean Journal of Agricultural Science
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• v.29 no.2
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• pp.78-90
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• 2002

This study was carried out to investigate whether peptide produced from wheat protein by enzyme hydrolysis can be used as a natural antimicrobial agent. Antimicrobial peptide was obtained from wheat protein by protease of 7 species. The produced antimicrobial peptide was purified through ultrafiltration, membrane filtration and HPLC, and molecular weight and amino acid sequence of the purified antimicrobial peptide were determined. Among hydrolysate produced from wheat protein by protease of 7 species, antimicrobial activity was observed for the peptide obtained from Asp. saito protease. The Asp. saito protease did production antimicrobial hydrolysate showing the highest antimicrobial activity at reaction condition of $37^{\circ}C$ and pH 6.0, but not at reaction condition above $50^{\circ}C$. Wheat protein hydrolysate was fractionated by membrane filtration and showed antimicrobial activity between molecular weight 1,000 - 3,000. The antimicrobial activity fraction obtained by membrane filtration was separated through HPLC and showed antimicrobial activity in the peak of retention time 31.1 - 31.8 min. Since after wheat protein protease hydrolysate was heated during 15 min at $121^{\circ}C$, antimicrobial activity was maintained, we could be conviction as heat-stable peptide. Molecular weight of antimicrobial peptide identified by MALDI-mass was 1,633. Amino acid sequence of antimicrobial peptide was cysteine, glycine, prolin, prolin, prolin, valine, valine, alanine, alanine and arginine.

• Korean Journal of Soil Science and Fertilizer
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• v.44 no.2
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• pp.200-205
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• 2011

This study was conducted to find the physico-chemical properties and the amino acid content of the pigs hoof hydrolysate, keratin protein and to investigate its fertilizer effect on the growth of crops. The keratin proteins such as pigs hoof were alkali-hydrolyzed to produce the hydrolysates. The chemical properties of the hydrolysate of pigs hoof was 6~7 of pH and $10{\sim}15dS\;m^{-1}$ of EC. Total amino acid contents released from the pigs hoof were 10.18%, respectively. The pot experiment was carried out for the cultivation of lettuce. The treatment design of these pot cultivation was composed of Control (compost + NPK), PHH-0.5, PHH-1.0, PHH-2.0 (${\times}2,000$ ; 1,000 ; 500 diluted solution of pig hoof hydrolysate). After lettuce cultivation, the pH values in all treatment soils were decreased than those in initial soils, and the exchangeable cation value was higher than that of control. In all PHH treatments, lettuce growth was better in the leaf length by 6~16% and the leaf width by 4~15% than in control. Therefore, the PHH solutions manufactured by hydrolysis process had plenty of amino acids, and among them PHH had the most abundant nutrients and amino acids with highest growth and yield effect on lettuce.

• Korean Chemical Engineering Research
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• v.52 no.1
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• pp.45-51
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• 2014

This is to study the effects of various pretreatment methods of agricultural residue, corn stover, and to compare the feature and pros and cons of each method including dilute sulfuric acid (DSA), soaking in aqueous ammonia (SAA), and ammonia recycle percolation (ARP). In order to convert corn stover to ethanol, various pretreatments followed by simultaneous saccharification and co-fermentation (SSCF) were tested and evaluated in terms of ethanol yield. With 3%, w/w of glucan loading using ARP-, DSA-, and SAA-treated solids, SSCFs using recombinant E. coli strain (ATCC$^{(R)}$ 55124) with commercial enzymes (15 FPU of Spezyme CP/g-glucan and 30 CBU/g-glucan enzyme loading) were tested. In the SSCF tests, 87, 90, and 78% of theoretical maximum ethanol yield were observed using ARP-, DSA-, and SAA-treated solids, respectively, which were 69, 58, and 74% on the basis of total carbohydrates (glucan + xylan) in the untreated corn stover. Ethanol yield of SAA-treated solid was higher than those of ARP- and DSA-treated solids. In addition, SSCF test using treated solids plus pretreated hydrolysate indicated that the DSA-treated hydrolysate showed the strongest inhibition effect on the KO11 strain, whereas the ARP-treated hydrolysate was found to have the second strongest inhibition effect. Bioconversion scheme using SAA pretreatment and SSCF can make the downstream process simple, which is suggested to produce ethanol economically because utilization of hemicellulose in the hydrolysate is not necessary.

• Fisheries and Aquatic Sciences
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• v.8 no.2
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• pp.109-112
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• 2005

A peptide that inhibits angiotensin-converting enzyme (ACE) was isolated from a hydrolysate of Manila clam (Ruditapes philippinarum) proteins prepared with thermolysin. Amino acid sequence of the peptide was determined to be Leu-Leu-Pro. Chemically synthesized Leu-Leu-Pro had an $IC_{50}\;value\;of\;158\;\mu{M}$. Peptides related to the Manila clam-derived peptide were synthesized to study the structure-activity relationships. The tetrapeptide, Leu-Leu-Pro-Pro, had a very weak effect on the enzyme. However, Leu-Leu-Pro-Asn showed no inhibitory activity.

• KSBB Journal
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• v.24 no.5
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• pp.415-419
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• 2009

In this study, the detoxification methods were evaluated for the removal of fermentation inhibitors from synthetic solution containing the composition similar to the lignocellulosic hydrolysate. The enzyme peroxidase and laccase were used as a biological treatment method. The physico-chemical methods such as adsorption and ion exchange were applied by using activated charcoal and ion exchange resins. The enzyme peroxidase showed a excellent removal of phenolic compounds. The 5-HMF and furfural were completely removed by activated charcoal. The anion exchange resin showed a good result for detoxification of acetic acid. The activated charcoal and ion exchange resins lead to a loss of sugars more or less. The choice of detoxification method must be made after considering the composition and inhibitors in hydrolysates.

• Fisheries and Aquatic Sciences
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• v.16 no.2
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• pp.71-78
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• 2013

Subcritical water hydrolysis was carried out in a batch reactor to produce valuable materials, such as low-molecular weight (MW) peptides and essential amino acids with antioxidant properties, from heat-dried squid viscera. Hydrolysis of squid viscera was performed at 160 to $280^{\circ}C$ for 3 min. The yield was increased by increasing the temperature and pressure, while the protein content of squid viscera hydrolysate decreased with increasing temperature. Low-MW peptides were detected in all hydrolysates by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The highest yields of free and structural amino acids in heat-dried squid viscera hydrolysate were at $160^{\circ}C$ and were $411.95{\pm}1.15$ and $346.62{\pm}1.25$ mg/100 g, respectively. All essential amino acids were detected in viscera hydrolysates; leucine was the most abundant. Antioxidant activities of hydrolysates were highest at $220^{\circ}C$. Greater than $98{\pm}0.26%$ of the ABTS antioxidant activity was retained in hydrolysates after long-term heat treatment.

• Preventive Nutrition and Food Science
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• v.13 no.3
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• pp.196-203
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• 2008

Hwangtae, dried Alaska pollack, is a major storage product in the fish processing industry. Hwangtae is prepared by removing the internal organs and drying outdoors during the cold witner months by allowing it to thaw during the daytime and re-freeze at night under sub-zero ($-10^{\circ}C$) conditions and gradually dry from December until the next April for around 5 months from Myungtae. In this study, ground Hwangtae was hydrolyzed using two proteolytic enzymes (pepsin and alcalase) which produced five soluble active peptides from Hwangtae (yellowish dried Pollack, Theragra chalcogramma) protein. Two different peptides with strong antioxidative activity were isolated from the hydrolysate using consecutive chromatographic methods of Sephadex G-25 gel, ion-exchange chromatography on a Sepharose-Sephadex C-25 gel, and high-performance liquid chromatography. The isolated peptides, APO1 and APO2, were composed of 16 and 13 amino acid residues, respectively. Both peptides contained a Gly residue at the C-terminus and the repeating motif Gly-Pro-Hyp. The peptide with a molecular weight less than 1,000 Daltons (APACE) obtained from enzymatic hydrolysates of Hwangtae exhibited the highest ACE inhibitory activity. The APACE peptides was composed of 4 amino acid residues (Gly-Leu-Leu-Pro). These results suggest that Hwangtae hydrolysates could be a good source of peptides with ACE inhibitory activity. Biochemical analysis indicated that two 70 kDa peptides (APG1 and APG2) isolated from the hydrolysate had gelatinoytic activity, which was shown to be a calcium dependent protease type as showed by gelatin SDS PAGE.

• 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 ($B_1,\;82.51{\pm}1.1){\gamma}/N-g\;and\;(B_2,\;115.29{\pm}1.5){\gamma}/N-g.$.

• Korean Journal of Pharmacognosy
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• v.12 no.2
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• pp.88-93
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• 1981

One hundred and forty-four extracts have been tested for the presence of saponins, using the method of froth formation, precipitate formation by acid hydrolysis, Liebermann-Buchard reaction on the acid hydrolysate, and hemolytic activity of the extracts. Among the samples tested, thirteen extracts showed positive saponin reaction in all the tests employed and one hundred and thirty-six showed positive in one or more tests of saponins. The results are tabulated.