• KSBB Journal
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• v.10 no.2
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• pp.137-142
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• 1995

When Escherichia coli W, which is able to utilize sucrose as a carbon source, harboring a high-copy-number plasmid (pSYL105) containing the Alcaligenes eultrophus polyhydroxyalkanoate(PHA) biosynthetic genes was cultured in a defined medium, the final poly(3-hydroxybutyric acid), PHB, concentration obtained was as low as $0.21g/\ell$. Ten different complex nitrogen sources were, therefore, examined for their ability to enhance PHB synthesis when supplemented to a defined medium. Addition of tryptone, casamino acids, casein hydrolysate, or soy bean hydrolysate enhanced PHB synthesis most significantly, resulting in more than 10 times higher PHB concentration compared with that obtained in a defined medium. Furthermore, PHB yield on sucrose was also increased by more than a 10 fold by the addition of these complex nitrogen sources, which suggested that PHB might be efficiently produced by the recombinant E. coli W(pSYL105) using sucrose as a carbon source.

• Journal of Life Science
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• v.10 no.2
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• pp.131-139
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• 2000

Lecithin-free egg yolk protein (EYP), the by-product of lecithin extraction from egg yolk, which is denatured with an organic solvent, would normally be discarded. In this study, the denatured protein was renatured with alkali, and hydrolyzed with Alcalase in order to utilize by-product. The hydrolysate was separated through a series of ultrafiltration membranes with molecular weight cut-off (MWOO) of 10, 5 and 1 kDa, and the antioxidative activities of the hydrolysates was investigated. The 5K hydrolysate, permeate from 5 kDa membrane, showed stronger antioxidative activity than 10 K and 1 K hydrolysate which were permeated from 10 kDa and 1 kDa membrane, in a linoleic acid autoxidation system. In addition, the optimum concentration of antioxidative activity for 5 K hydrolysate was 1%, and the activity was about 37% higher as compared with α-tocopherol. The synergistic effect was also increased by using the hydrolysates with α-tocopherol.

• Korean Journal of Pharmacognosy
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• v.33 no.4 s.131
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• pp.312-318
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• 2002

Effect of the acid hydrolysate of silk fibroin on obesity was investigated in obese(057BL/KsJ-db/db) mice. After 8 weeks feeding of 1%(w/w) or 3%(w/w) fibroin hydrolysate, the extents of reduction in body weight were significantly higher than that of obese control. The weight reduction in female mice was higher than that in male mice. Plasma leptin in male mice increased up to 1.8-fold higher level than obese control by feeding hydrolysate. In case of female mice, however, it rather decreased with increased feeding concentration of hydrolysate. From the results of high glycine and serine contents of peptide fractions contained in fibroin hydrolysate, it was inferred that fibroin peptides might affect xylosyltransferase(XT) activity on chondroitin sulfate synthesis causing to change susceptibility of adipocytes to hormones such as insulin followed by the reduced leptin synthesis in female mice. The result of the higher lipolysis in hydrolysate-fed group than obese control indicated that the reduction in body weight was due to the increased lipolytic activities in male and female mice in common.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.1
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• pp.35-39
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• 1998

An enzymatic process was developed to produce protein hydrolysater form defatted soya protein. Various unit operations were tried, and the effects of pre- and post-treatments on the product characteristics such as degree of hydroylsis (DH), free amino acid content (%FAA) and average molecular weight (MW) were investigated. The use of acid washes showed no difference in %DH. Increasing pH during pre-cooking gave lower %DH. Alkaline cooking made too much insoluble protein, thus the protein yield was too small. A better hydrolysis with more acceptable taste was obtained when the combination of Neutrase/Alcalase/Flavourzyme was used in place of Alcalase/Flavourzyme combination; Untoasted defatted soya was more effective on the proteolysis than toasted one. The MW of the evaporated and spray dried product was higher than that of undried product, due to precipitation of low-solubility components. When ultrafiltration and the product concentration carried out the product separation by reverse osmosis, the solubility and the taste of the product were improved. The difference between enzyme hydrolysate and acid hydrolysate was significant in free amino acid composition, especially in tyrosine, phenylalanine, glutamine and asparagine.

• Journal of the Korean Chemical Society
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• v.7 no.1
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• pp.6-12
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• 1963

Amino acid composition of Makjang was determined by combined usage of ion exchanged resin and paper chormatography in the following states. a. A fraction soluble in water b. Hydrolysate of the whole Makjang c. Same as a. (p.p.t. formed by tungstic acid or trichloroacetic acid being removed) d. Hydrolysate of c. (T and TCA) By comparing amino acid composition of Makjang with that of its raw material, we found that decomposition of essential amino acids during brewing is slight. From the amino acid composition of a,b,c,d, we discussed the ratio of amino acid liberation during brewing and assumed that Makjang contains peptide-like substances composing of glutamic acid and aspartic acid.

• Fisheries and Aquatic Sciences
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• v.13 no.1
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• pp.84-87
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• 2010

A peptide that inhibits HIV-1 protease was isolated from a hydrolysate of oyster (Crassostrea gigas) proteins digested with thermolysin. The peptide was using membrane filtration, gel permeation chromatography, ion exchange chromatography, and reverse-phase high performance liquid chromatography. Amino acid sequence of the peptide was determined to be Val-Phe-Glu-Leu. Chemically synthesized Val-Phe-Glu-Leu showed an $IC_{50}$ value of 106 ${\mu}M$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.35 no.1
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• pp.97-104
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• 2002

Protein hydrolysate was prepared as a natural flavor stock from the sharp toothed eel (Muraenesox cinereus) mince using com-mercially available proteolytic enzymes, Alcalase, Neutrase, Protamex, and Flavourzyme. A 6 hr hydrolysis of mince, to which water of the equal weight of the mince was added, with $2\%$ (w/w, protein weight) Elavourzyme at $50^{\circ}$ yielded a hydrolysate of the highest acceptability. Removing the access lipid in liquified hydrolysate (not dehydrated) after enzyme hydrolysis, five times repetitive extraction using n-hexane (liquified hydrolysate : n-hexane=4 : 1, v/v) was effective, resulting in less than $1\%$ lipid content of the dehydrated-hydrolysate. The amino acid composition of the hydrolysate (prepared with Flavourzyme) was similar to that of the starting material. Hydrolysis led to an increase in concentration of not only total free amino acid but also free amino acid such as serine, glutamic acid, alanine, and methionine responsible for umami taste, especially up to about 40 times for methionine. Major free amino acids in amount were leucine, phenylalanine, valine, alanine, and isoleucine and they comprised about half of the total free amino acids, Moisture adsorption, fat adsorption, emulsifying capacity, and foaming capacity of the hydrolysate were 870.1 $\pm$ $7.9\%$, 352.0$\pm$ $5.3\%$, 50.3 $\pm$ $1.2\%$, and $87.5\pm$ $2.5\%$, respectively, and solubility was 83$\~$$84\%$ at acid pH range of 2$\~$4.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.2
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• pp.164-172
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• 2001

The angiotensin-I converting enzyme (ACE) inhibitors from laver hydrolysate was isolated. Among the 13 kinds of proteases, Maxazyme NNP was most effective for preparing the high ACE inhibitory compound. In extraction conditions of ACE inhibitory peptide from laver hydrolysate, ACE inhibitory activity of hydrolysate treated with diethylether for decolorization and that of $70\%$ ethanol soluble fraction among the different ethanol concentrations were higher than other preparations. Low molecular fraction less than 3,000 dalton of layer hydrolysate separated by ultrafiltration had the highest ACE inhibitory activity, for further separation of ACE inhibitory peptide from laver hydrolysate, gel filtration chromatography (Sephadex G-25), reverse-phase HPLC (ODS & Vydac C-18) and gel permeation chromatography (Superdex Peptide HR) were performed. The molecular mass of the ACE inhibitory peptide fractions of gel permeation chromatography determined by electrospray-mass spectrometer were 413.48 (S1O2V2V1P),346.86 (S1O2V2V2P) and 320.32 (S2O6V3V1P) dalton and their amino acid sequence were Val-Gln-Gly-Asn, Thr-Glu-Thr and Phe-Arg, respectively.

• Microbiology and Biotechnology Letters
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• v.30 no.1
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• pp.39-45
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• 2002

It was found that the peptides originated from the hydrolysates of silk fibroin have in vitro immunostimulating effects in murine macrophage RAW264.7 cells. The stimulation effects on nitric oxide (NO) production resulted from treatments of acid or enzymatic hydrolysates were measured. The silk fibroin preparation isolated from cocoon was most efficiently digested by acid hydrolysis. Even though the sole treatment of acid hydrolysate stimulated the NO production in dose-dependent pattern, a part of its activity was found to be caused by the contaminated endotoxin, LPS. When each endotoxin-free hydrolysates obtained by filtering it through an ultrafiltration membrane of molecular weight (MW) cut-off 10,000 to eliminate LPS was used, the peptic hydrolysate with lowest degree of hydrolysis showed the highest activity. The fractions of peptic hydrolysate with MW ranges of 1,000∼10,000, 500∼1,000 and below 500 also showed a higher MW-higher activity correlation. From the analyses of amino acid composition of each hydrolysate, it was found that the contents of arginine, lysine, alanine and glycine residues affected the activity level of hydrolysate. The results of this study showed a possibility of utilizing fibroin as a source for immunostimulating (chemopreventive) functional peptides.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.917-922
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• 2009

This study investigated the effects of steaming on the antioxidative activities of ray hydrolysates in vitro. Based on the results of 1,1-diphenyl-2-picrylhydrazyl (DPPH) assay, steamed ray hydrolysate possessed significantly higher antioxidative activities than raw ray hydrolysates (p<0.05). The 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity of steamed ray hydrolysate by pancreatin was slightly lower than raw ray hydrolysate at all concentrations. Raw ray hydrolysate displayed moderate hydroxyl radical scavenging activity, while steamed ray hydrolysate showed a greater increase in hydroxyl radical scavenging activity than raw ray hydrolysate at concentrations above 21.33 mg/mL, and it reached 58.21% at 42.67 mg/mL. The results of this study show that ray hydrolysates have potent free radical scavenging activities and reducing power, and the steaming has a partial impact on the antioxidative activity of ray hydrolysates.