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

• Korean Journal of Agricultural Science
• /
• v.22 no.1
• /
• pp.62-68
• /
• 1995

This study was carried out to examine splitting, developmental capacity and rapid freezing of blastomeres separated from 2-, 4-, 8-cell and morula from porcine embryos. The results obtained in this study were summerized as follows : 1. The successful splitting rate by pronase was 85.7% in 2-cell embryos(average splitting rate, 68.0%), and by manipulator was 76.6% and 74.3% in 2- and 4-cell embryos. 2. The developmental capacity rates of splitted embryos by the pronase treatment were 24.1%, 20.4%. 25.5% and 26.6% in 2-, 4-, 8-cell and morula, and by manipulator were 36.4%, 39.5%, 36.1% and 41.9%, respectively. 3. The successful results of in vitro culture after frozen-thawed of splitted embryos were 16.1%(glycerol) in 2-cell, 16.7%(DMSO) in 4-cell and 27.6%(ethyleneglycol) in morula, respectively.

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

• The Korean Journal of Food And Nutrition
• /
• v.8 no.3
• /
• pp.192-198
• /
• 1995

For the production of EMC, various professes and lipases were used to hydrolyse cheese sulk. The optimal conditions of various proteases were as follows, pronase-3$0^{\circ}C$, p14 7.0, pancreatln-4$0^{\circ}C$, pH 8.0, pacific protease-3$0^{\circ}C$, pH 7.0 and protease from Asp. sp. -5$0^{\circ}C$, pH 8.0. The optimal conditions of various lipases were as follows ; pancreatic lipase-5$0^{\circ}C$, pH 8.0, palatase ML-5$0^{\circ}C$, pH 7.0 and lipase form Candida -4$0^{\circ}C$, pH U.0. After hydrolysation under optimal conditions, the amounts of free amino acid and free fatty ac14 were increased with reaction time. Hydrolysates of pacific protease and pronase were showed high amount of free amino acid(0.67mg/ml and 0.74mg/ml). Especially EMC had high amount of glutamic acid and leucine. Lipase from Candida cylindracea produced high amount of free fatty acid (24.63 mg/ml) Butyric acrid, palmitic acid, stearic acid and oleic acid among free fatty acids were showed high amounts. Sensory evaluation of various MC were tasted nth 8 panelist. EMC produced with pancreatic lipase was most bitterness and EMC produced with palatase ML was best acceptable cheese flavor.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.34 no.5
• /
• pp.515-520
• /
• 2001

The anticoagulant activities of fucoidan fractions extracted from Sporophylls of Undaria pinnatifida, Laminaria religiosa, Hizikia fusiforme and Sargassum fulvellum were studied to assess the relationship between chemical characteristics and the activities. Crude fucoidans extracted with diluted HCl solution (pH 2.0) at $65^{\circ}C$ were precipitated with cetylpyridinum chloride and then fractionated by dissolving the precipitated complex with increasing $CaCl_2$, concentrations (1.0 M, 1.5 M, 3.0 M). The anticoagulant activities of the fractions with respect to activated partial thromboplastin (APTT) increased with increase in their sulfate content and Undaria finnatifida Fr-3.0 fraction, prepared by dissolving with 3.0 M $CaCl_2$ solution, exhibited the highest activity. The Undaria finnatifida Fr-3.0 fraction was further modified with pronase and laminase. The pronase and laminase treatment decreased protein and glucose content and the APTT activity was higher than that or parent Undaria finnatifida Fr-3.0 fraction. The pronase and laminase modified Undaria finnatifida Fr-3.0 was composed of fucose, galactose, mannose, sulfate, uronic acid in the approximately molar ratio of 1.00 : 1.30: 0.03 : 2.70 : 0.08.

• Korean Journal of Food Science and Technology
• /
• v.16 no.2
• /
• pp.211-217
• /
• 1984

To study affinity of proteolytic enzymes to soy proteins, the physicochemical and functional properties of enzymatically modified protein products, kinetic parameters and degree of hydrolysis were measured using trypsin, alcalase (serine type protease) and pronase. Bacterial alcalase and pronase showed much greater affinity to soy protein than animal intestinal trypsin. This effect was very significant when unheated soy isolate was used as a substrate. Specific activities of these enzymes decreased with the increment of substrate concentration (over 2.0%, w/v) when heat denatured soy protein was used as a substrate. However, the decrease in specific activity was negligible at substrate concentrations lower than 2.0%. Polyacrylamide gel electrophoretic results showed that the pattern of 2S protein band changed distinctly in alcalase hydrolysis as compared with those of trypsin and pronase. Protein solubilities of alcalase and pronase hydrolyzates increased by 25-30%, at their pI (pH 5.0) over the control. Virtually no change was observed in solubility by trypsin hydrolysis. Heat coagulability and calcium-tolerance of the protein increased by enzymatic hydrolysis. No clear tendency, however, was observed for emulsion properties, foam expansion and the amount of free -SH groups. The enzyme treatment considerably decreased foam stability.

• Korean Journal of Microbiology
• /
• v.28 no.1
• /
• pp.65-70
• /
• 1990

The objective of the current study is to elucidate the biological roles of proteinase inhibitor in microorganisms. As the first step, a strain of Streptomyces fradiae was selected as a producer of extracellular proteinase inhibitor. The proteinase inhibitor was purified from culture broth through ultrafiltration, gel-filtration and ion-exchange chromatography. Molecular weight of the proteinase inhibitor was estimated to be 16, 800 by SDS polyacrylamide gel electrophoresis. It was found that the proteinase inhibitor inhibited only alkaline serine proteinases such as subtilisin, $\alpha$-chymotrypsin and Promase E but not trypsin and other proteinases. The mode of inhibition against Pronase E with succinyl-phenylalanine-p-nitroanilide as a substrate was competitive.

• 대한생식의학회:학술대회논문집
• /
• 2001.06a
• /
• pp.75-75
• /
• 2001

• Korean Journal of Environmental Biology
• /
• v.29 no.4
• /
• pp.305-311
• /
• 2011

The distribution of flocculating activity of culture broth was examined and the major constituent with flocculating activity was identified. Most of flocculating activity was found in culture broth without cells. As the activity was maintained by the digestion with pronase, it suggests that the activity is due to the polysaccharide. The bioflocculant obtained from $Lactobacillus$ $jensenii$ YW-33 was precipitated by 60~80% EtOH fractionation (LJ-80). LJ-80 was separated by ion-exchange chromatography using DEAE-Toyopearl 650C and LJ-80-II showed more potent flocculating activity than those of other fractions. The major activity fraction LJ-80-II was further purified on the gel permeation using Sepharose CL-6B to LJ-80-II-1. GPC (Sepharose CL-6B) and HPLC were used to determine whether LJ-80-II-1 has a homogenecity. The molecular weight of purified LJ-80-II-1 was estimated over 800,000 dalton by gel permeation chromatography. Purified LJ-80-II-1 contained 98.4% total sugar, 0.6% protein. Main sugar of purified LJ-80-II-1 was composed of mannose : galactose : glucose with a molar ratio of 1.61 : 0.25 : 1.00.

• Applied Biological Chemistry
• /
• v.39 no.2
• /
• pp.159-164
• /
• 1996

Screening of anticoagulant activity was conducted for the hot water extracts of 73 kinds of medicinal herbs, 41 kinds of Korean edible plants, and 5 kinds of sea weeds using plasma recalcification test(Tr). In the first screening several extracts of the plants, Alisma calndiculatum, Corydalis ternata Panax notoginseng, Allium sativum, Ganderma luidum, Codium fragile, showed high activities. When the plants were reextracted with various solvent conditions, acidic water extracts of Codium fragile showed the highest activity in APTT. A crude polysaccharide fraction(CF-1) was prepared by methanol reflux, ethanol precipitation, dialysis and Iyophilization of the acid extracts. CF-1 comprised 80.8% total sugar consisting of arabinose, galactose and glucose as the main monomers, 8.7% protein, and 13.3% sulfate. The anticoagulant activity of CF-1 was not changed by pronase digestion, but decreased by periodate oxidation, and this indicated that the anticoagulant activity was attributed to the polysaccharide portion.