• The Korean Journal of Food And Nutrition
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• v.8 no.4
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• pp.335-343
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• 1995

In order to enhance the utility of alaska-pollack, the optimum conditions for the preparation of pronase hydrolysate. The optimum temperature and pH for the hydrolysis of alaska-pollack by pronase were 4$0^{\circ}C$ and pH 7.0. The reaction time and enzyme concentration were 4 hr and 1,000 units per g of substrate. Under the above optimum conditions alaska-pollack was hydrolysed by pronase yielding a hydrolytic degree of about 89eye. The bitterness and hyrophobicity of pronase hydrolysate were decreased with increasing reaction time. Hydrophobic amino acids(Tyr, Met, Ala, flu, Leu, and Phe) were increased for 2 hr, but fur thor hydrolysis was showed decrease of hydrophobic amino acids content. Palatable amino acids (Asp, Glu, Pro, Ser, Thr and Gly) were increased with hydrolysis time.

• Applied Biological Chemistry
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• v.35 no.5
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• pp.339-345
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• 1992

In order to enhance the processing quality and utility of alaska-pollack meat, the optimum conditions for the preparation of pronase hydrolysate and the synthesis of plastein were investigated. The optimum temperature and pH for the hydrolysis of alaska-pollack by pronase were $40^{\circ}C$ and pH 7.0. The reaction time and enzyme concentration were 4 hr and 1,000 units per g of substrate. Under the above optimum conditions alaska-pollack was hydrolyzed by pronase yielding a hydrolytic degree of about 89%. Pronase hydrolysate was employed as substrate for plastein synthesis. The 30% pronase hydrolysates were adjusted to pH 7 for fruit-bromelain and pH 5 for stem-bromelain, and then plastein were synthesized by 1% bromelain at $40^{\circ}C$ for 24 hr. The plasteins synthesized by fruit- and stem-bromelain were consisted of peptides having average peptide length of 22.6 and 20.8 under the optimum synthetic conditions. The plastein synthesis reaction reduced considerably the bitterness of pronase hydrolysate.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.49 no.5
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• pp.594-599
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• 2016

Infection with HIV (Human immunodeficiency virus), over time, develops into acquired immunodeficiency syndrome (AIDS). The development of non-toxic and effective anti-HIV drugs is one of the most promising strategies for the treatment of AIDS. In this study, we investigated the anti-HIV-1 activity of gelatin hydrolysates from Alaska pollack skin. Gelatin hydrolysates were prepared using four enzymes (alcalase, flavourzyme, neutrase, and pronase E). Among these, the pronase E gelatin hydrolysate was found to inhibit HIV-1 infection in the human T cell-line MT4. It exhibited inhibitory activity on HIV-1_IIIB-induced cell lysis, reverse transcriptase activity, and viral p24 production at noncytotoxic concentrations. Moreover, it decreased the activation of matrix metalloproteinase-2 (MMP-2) in vitro. Because HIV infection-induced activation of MMP-2 can accelerate collagen resolution and collapse of the immune system, pronase E gelatin hydrolysate might prevent the activation of MMP-2 in cells, resulting in collagen stabilization and immune cell homeostasis consistent with anti-HIV activation. These results suggest that pronase E gelatin hydrolysate could potentially be incorporated into a novel therapeutic agent for HIV/AIDS patients.

• KSBB Journal
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• v.6 no.4
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• pp.327-336
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• 1991

A study on the optimum hydrolysis conditions of fish skin through the aid of enzymes and the development of a natural seasoning using the hydrolysate has been carried out for the effective utilization of fish skin. Using the "pH-drop" techniques the collagenase and pronase were identified as most suitable for this purpose. The $K_m$ and $V_{max}$ values of pronase were 1.82 mgN/ml and 0.06 mgN/mL/min, respectively. The hydrolysis conditions of the cod skin for the pronase were as follows: reaction temperature, $50^{\circ}C$; reaction time, 3hrs; pH 6; enzyme concentration, 0.03%. The degree of hydrolysis at these conditions was 76.8%. But after hydrolyzing cod skin with collagenase for 1hr, when the pronase was treated, the degree of hydrolysis was 83.13%. The molecular weight of the hydrolysate was 8,000 daltons. Among the amino acids in the hydrolysate, glycine(27.95%), glutamic acid(10.94%), proline(7.39%), aspartic acid(9.47%) and serine(7.39%) were responsible for 64.23% of the total amino acids. But valine, methionine, isoleucine, leucine, phenylalanine and histidine having a bitter taste were only 13.05%. From the results of the sensory evaluation, the imitation sauce which was made of 20% fermented soy sauce prepared from the hydrolysate was at least similar to the traditional soybean sauce in product quality. The complex seasoning containing 31.7% of the hydrolysate was nearly equal to complex seasonings on the market, too.

• Fisheries and Aquatic Sciences
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• v.12 no.3
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• pp.163-170
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• 2009

This study was conducted to obtain the gelatin fraction with a high anti oxidative activity from Alaska pollock surimi by-products using a two-step enzymatic hydrolysis and ultrafiltration. Among gelatin hydrolysates from refiner discharge of Alaska Pollock surimi, the highest antioxidative activity (81.5%) resulted from gelatin hydrolysate sequentially treated with Pronase E and Flavourzyme each for 2 hr. However, no difference was seen in the anti oxidative activity of the second hydrolysate (Pronase E-/Flavourzyme-treated hydrolysate) when compared to the permeate fractionated through a 10-kDa membrane. The results suggest that the Pronase E-/Flavourzyme-treated hydrolysate from refiner discharge gelatin of Alaska pollock surimi can be used as a supplementary raw material for improving health functionality.

• Korean Journal of Food Science and Technology
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• v.28 no.4
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• pp.678-683
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• 1996

The purpose of this study was to elucidate characteristics of hydrolysates from file-fish flesh with various proteases. File-fish flesh was chopped, homogenized with water, and hydrolysed by 8 different kinds of commercially available protease. High production of peptide was observed in bromelain and neutrase treatment. On the other hand, large amount of free amino acid was observed in esp/sav and pronase treatment. Neutrase and pancreatin hydrolysate contained large amount of 5'-GMP. Organoleptic studies showed that the bromelain, esp/sav and protease hydrolysate had strong bitter taste, while pronase and esp/sav hydrolysate had strong umami taste. From these results, pronase was found to be suitable enzyme for producing file-fish hydrolysate.

• Bulletin of the Korean Chemical Society
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• v.20 no.11
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• pp.1299-1302
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• 1999

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) was used to demonstrate cross-linking of peptides induced by transglutaminase. The presence of ε-( Υ-glutamyl)lysine isopeptide cross-link in the acid hydrolysate of the cross-linking reaction mixture was also demonstrated by MALDI-TOF-MS without prior separation. MALDI-TOF-MS quickly provided peptide mass maps after pronase digestion of the cross-linked peptide adduct, which enabled us to monitor the hydrolytic sequence. Pronase appears to preferentially hydrolyze peptide bonds distant from the cross-link before hydrolyzing peptide bonds around the cross-link. The results suggest that pronase digestion followed by MALDI-TOF-MS could be used for determination of amino acid sequence around a modification site.

• KSBB Journal
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• v.15 no.6
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• pp.635-643
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• 2000

To compare the antioxidative activities of fish skin and bovine skin gelatin hydrolysate, gelatin hydrolysates from Alaska pollack and bovine skin were prepared by various enzymatic hydrolysis methods (1st step, Alcalase; 2nd step, pronase E; 3rd step, collagenase) using a continuous three-step membrane reactor. The molecular weight distributions of the 1st, 2nd and 3rd step hydrolysates were 7∼10 kDa, 2∼5 kDa and 0.7∼0.9 kDa, respectively. The antioxidative activity of fish skin gelatin hydrolysate was stronger than that of bovine skin gelatin hydrolysate, and in particular, both of 2nd step hydrolysates showed more antioxidative activity than hydrolysates of any other step. The optimum antioxidative activity concentration of the 2nd step hydeolysates of fish and boving skin were 1% (w/w) in a linoleic acid water-alcohol emulsion. In cultured cells exposed to t-butyl hydroperoxide (t-BHP), the 2nd step hydrolysate of fish skin gelatin delayed cell death most. These results suggest that the antioxidative activity of fish skin gelatin hydrolysate is higher than that of bovine skin gelatin hydrolysate because of their different amino acid contents.

• BMB Reports
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• v.34 no.3
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• pp.219-224
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• 2001

To identify the antioxidative peptides in the gelatin hydrolysate of bovine skin, the gelatin was hydrolyzed with serial digestions in the order of Alcalase, pronase E, and collagenase using a three-step recycling membrane reactor. The second enzymatic hydrolysate (hydrolyzed with pronase E) was composed of peptides ranging from 1.5 to 4.5 kDa, and showed the highest antioxidative activity, as determined by the thiobarbituric acid method. Three different peptides were purified from the second hydrolysate using consecutive chromatographic methods. This included gel filtration on a Sephadex G-25 column, ion-exchange chromatography on a SP-Sephadex C-25 column, and high-performance liquid chromatography on an octadecylsilane chloride column. The isolated peptides were composed of 9 or 10 amino acid residues. They are: Gly-Glu-Hyp-Gly-Pro-Hyp-Gly-Ala-Hyp (PI), Gly-ProHyp-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly (PII), and Gly-ProHyp-Gly-Pro-Hyp-Gly-Pro-Hyp (PIII), as characterized by Edman degradation and fast-atom bombardment mass spectrometry. The antioxidative activities of the purified peptides were measured using the thiobarbituric acid method, and the cell viability with a methylthiazol tetrazolium assay The results showed that PII had potent antioxidative activity on peroxidation of linoleic acid. Moreover, the cell viability of cultured liver cells was significantly enhanced by the addition of the peptide. These results suggest that the purified peptide, PII, from the gelatin hydrolysate of bovine skin is a natural antioxidant, which has potent antioxidative activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.5
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• pp.519-524
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• 1992

purified rapeseed(Brassica napus var. Youngsan) protein was hydrolyzed by pronase. The hyrolysate protein was investigated for the some physicochemical and functional properties. UV and intrinsic fluorescence spectra of the hydrolysate showed the maximum absorption at 274nm and 360nm respectively. Intensity of yellow color decreased in the process of hydrolysis and the surface hydrophobicity decreased up to fourfold. The main bands of hydrolysate by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) were observed at 14,000 to 12,000 dalton molecular weight. Solubilities of hydrolyzed protein increased by 10~15% compared to those of unhydrolyzed protein at acidic pH. In the hydrolysate, while absorption of both water and oil, foam expansion and emulsion stability were increased, absolute viscosity, heat coagulation, calcium coagulation, foam stability and emulsion activity were decreased.