• Food Science of Animal Resources
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• v.40 no.2
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• pp.172-182
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• 2020

In the present study, we determined the degree of hydrolysis (DH) of porcine blood plasma proteins, albumin, and globulin hydrolyzed by six proteases (alcalase, neutrase, flavourzyme, protamex, trypsin, and papain) for various reaction times. Moreover, antimicrobial activities of hydrolysates against five pathogenic microorganisms (Bacillus cereus, Staphylococcus aureus, Salmonella Typhimurium, Escherichia coli, and Shigella flexneri) were investigated. Alcalase, trypsin, and papain hydrolysates of the three porcine blood proteins showed higher DH values than hydrolysates produced by the other three proteases. DH of the three porcine blood proteins hydrolyzed by the six proteases failed to increase after 2 h of hydrolysis. In antimicrobial tests, hydrolysates (hydrolysis time of 2 h) showed antibacterial activity only against B. cereus. Albumin hydrolysates showed higher antimicrobial activity than globulin and plasma hydrolysates. Albumin hydrolysates obtained with flavourzyme, protamex, and trypsin showed higher antimicrobial activity than those obtained with the other three proteases.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.3
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.35 no.2
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• pp.39-45
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• 2003

This study was performed to develop the new type enzyme immobilization sheet from carboxymethylated refiner mechanical pulp (CRMP) substrate. Enzyme immobilization was attempted to couple carboxyl groups of CRMP with amino groups of the enzyme, trypsin, through the reaction of carbodiimide reagent, 1-ethyl-3-(3-dimethyl aminopropyl)-carbodimide (EDC ). Immobilization carrier, water insoluble CRMP fraction (CRMP-IS), was successfully reacted with the enzyme, formed peptide linkage like -CONH- at 1680$cm^{-1}$ / and new ester linkage like -COO$CH_3$, methylester at 1735$cm^{-1}$ /, and produced enzyme immobilized substrate (CRMP-IST). The enzyme immobilized handsheet was prepared by mixing the above chelated enzyme immobilized substrate(CRMP-IST) with kraft pulp by paper sheet machine like papermaking process. The sheet weight and strength were increased with increasing dosage of CRMP-IST, and decreased at more than 10％ mixing of CRMP-IST, but higher than the controls. Concerning activities of immobilized trypsin(CRMP-IST) sheet by caseinolysis, the teared-off sheet with shaking was shown higher enzyme activities than sheet shape without shaking. In conclusion, this enzyme immobilized sheet would be expected easy handling for practical application and reutilization.

• Applied Chemistry for Engineering
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• v.5 no.2
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• pp.321-326
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• 1994

The water-soluble polyphosphazene possessing ether side groups was exposed to ${\gamma}-rays$ to prepare hydrogens with good water-swellability. The physical strength of these hydrogels could be controlled by irradiation dose of ${\gamma}-rays$. Trypsin and water-soluble polyphosphazene were irradiated together by ${\gamma}-rays$ for entrapment of enzymes into hydrogel networks. The activities of immobilized trypsin were examined spectrophotometrically after the reaction with N-${\alpha}$-benzoyl-1-arginine-p-nitroanilide in phosphate buffer. The immobilized trypsin was found to have good activity yield and suability after at least 500 hours.

• The Korean Journal of Zoology
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• v.33 no.1
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• pp.119-125
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• 1990

A Potent inhibitor of trypsin and other various serine proteases including chymotrypsin, elastase, kallikrein, plasmin and subtilisin, has been purified to homogeneity from chick skeletal muscle by convendonal chromatographic procedures. The Inhibitor has an apparent molecular weight of 66, 000 dalton as determined by gel filtration. When the purified inhibitor was electrophoresed in the presence of sodium dodecyl sulfate, there appeared rwo protein bands having molecular weights of 66, 000 and 64, 000 dalton. The 64, 000 dalton protein seems to be the product of 66, 000 dalton protein by a lin'ited proteolysis during the purification procedure or in viuo. Thus, it seems to consist of a single polypeptide. The inhibitor appeared to be glycoprotein and have an isoelectric point of 7.4. It contains relatively large amount (8.33 mole%) of cysteine residues.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.88.3-89
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• 2003

Acanthoic acid (AA) is a pimaradiene diterpene isolated from the Korean medicinal plant, Acanthopanax koreanum (Araliaceae), which has been traditionally used as a tonic and sedative as well as in the treatment of rheumatism and diabetes in korea. Proteinase-activated receptor-2 (PAR-2) agonist trypsin plays a role in inflammation, and human leukemic mast cells (HMC-l) express PAR-2. In the present study, the effect of acanthoic acid on production of tumor necrosis factor-${\alpha}$ (TNF-${\alpha}$) and tryptase in trypsin-stimulated HMC-1 was examined. (omitted)

• Food Science and Biotechnology
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• v.18 no.3
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• pp.706-711
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• 2009

Lysozyme was treated with digestive enzymes and the production of interleukin 8 (IL-8) was measured in Caco-2 cell with the peptides from lysozyme upon stimulating with lipopolysaccharide (LPS) to investigate the overall anti-inflammatory activity of lysozyme when it is in digestive tracts. Lysozyme reduced IL-8 production, and the peptides from pepsin hydrolysis of lysozyme had the similar effect. The products of trypsin digestion of lysozyme had no effect on the reduction of IL-8 production while those of pepsin-trypsin hydrolysis did. The effectiveness of lowering IL-8 production was not different by time of the peptide addition. When Caco-2 cells were pre-incubated with peptides for 24 hr, the reduction effects were observed from the peptides from pepsin hydrolysis, indicating that some of the peptides are still remaining in the cells. Therefore, it can be concluded that the IL-8 reduction effect of lysozyme against LPS still remained even after the pepsin and trypsin hydrolysis.

• Journal of Microbiology
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• v.33 no.4
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• pp.315-321
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• 1995

The relationship between morphological differentiation and production of trypsin-like protease (TLP_ in streptomycetes was studied. All the Streptomyces spp.In this study produced TLP just before the onset of aerial mycelium formation. Addition of TLP inhibitor, TLCK, to the top surface of colonies inhibited aerial mycelium formation as well as TLP inhibitor, TLCK, to the top surface of colonies inhibited aerial mycelium formation as well as TLP activity. Addition of 2% glucose to the Bennett agar medium repressed both the aerial mycelium formation and TLP production in S. abuvaviensis, S. coelicolor A3(2), S exfoliatus, S. microflavus, S. roseus, s. lavendulae, and S. rochei. However the addition of glucose did not affect S. limosus, S. felleus, S. griseus, S. phaechromogenes, and S. rimosus. The glucose repression on aerial mycelium formation and production of TLP was relieved by the addition of glucose anti-metabolite (methyl .alpha.-glucopyranoside). Therefore, it was concluded that TLP production is coordinately regulated with morphological differentiation and TLP activity is essential for morphological differentiation in streptomycetes. The proposed role of TLP is that TLP participates in the degradation of substrate mycelium protein for providing nutrient for aerial mycelial growth.

• Applied Biological Chemistry
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• v.38 no.3
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• pp.248-253
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• 1995

Optimum conditions for the enzymatic hydrolysis of isolated sesame meal protein were investigated. Optimum conditions by papain were $60^{\circ}C$, pH 6.0, 3% enzyme concentration to substrate and 1.5% substrate concentration, respectively. The optimum operating conditions using pepsin were $55^{\circ}C$, pH 9.0, 3% enzyme concentration to substrate and 1% substrate concentration. The optimum operating conditions using trypsin were $60^{\circ}C$, pH 9.0, 1% enzyme concentration to substrate and 1% substrate concentration.

• The Korean Journal of Food And Nutrition
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• v.7 no.2
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• pp.151-158
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• 1994

This study was carried out to clear up the cause of low-acid producing phenomenon occurred In non-fat dry milk during liquid-yoghurt fermentation by Lactobacillus case, and to present its improving methods. All samples of non-fat dry milks which were low in TCA-soluble peptides showed low-acid production, but those high in TCA-soluble peptides showed high-acid production. The addition of trypsin-hydrolysate of Na-caseinate to non-fat dry milk showed some improving effect on acid production but that of papain-hydrolysate did not show any improving effect and that of bacterical neutral protease-hydrolysate showed some inhibitory effect. The improving effects on growth and acid production of lactic acid bacteria were more prominent when the trypsin-hydrolysate of Na-caseinate was added. to such fermenting system in which the levels of TCA-soluble peptides and the proteolytic ability of starter bacteria were abnormally low. The liquid-yoghurt made with non-hydrolysed Na-caseinate and defective non-fat dry milk showed precipitate occurrence but that with trypsin-hydrolysate of Na-caseinate and defective non-fat dry milk did not make any precipitate during storage as with normal non-fat dry milk.