• Fisheries and Aquatic Sciences
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• v.6 no.3
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• pp.105-109
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• 2003

Fifty four strains of pathogenic vibrios were isolated from the Gwangan Beach from May to October, 2002. The isolated vibrios were composed of 7 different species: Vibrio parahaemolyticus, V. cholerae non-O1, V. alginolyticus, V. vulnificus, V. hollisae, V. fluvialis, ane V. mimicus. In the detection rate, V. parahaemolyticus was most predominant as $46\%$(25/54). From the isolated strains, only 25 strains have hemolytic activity or 25 strains only proteolytic activity on agar plates. Eleven strains showed both hemolytic and proteolytic activity. No strains showed urease activity. All strains of V parahaemolyticus did not show hemolytic activity, while V. cholerae non-O1 strains showed $\beta$ hemolytic activity. Kanagawa phenomena of pathogenic vibrios did not accord with hemolytic activity of the culture supernatant at the late log phase. Some strains showed high hemolytic activity despite having proteolytic activity, but some weak hemolytic activities despite having no proteolytic activity.

• Journal of Pharmaceutical Investigation
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• v.19 no.4
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• pp.203-212
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• 1989

A proteolytic enzyme was extracted from Sarcodon aspratus (Berk) S. Ito by percolation method. Proteolytic activity of the extracted proteolytic enzyme (SAP) was compared with several digestives containing proteolytic enzymes. Potency of SAP was higher than that of the other digestives except for protease. The optimum pH ranse of SAP was similar to that of pancveatin and protease. SAP was more stable than pancreatin and protease under various temperature, alkaline pH, and metal ions. Bovine serum albumin hydrolysing activity of SAP was equivalent to that of pancreatin and protease in small intestine of rats. SAP demonstrated lower adsorption to antacids than pancreatin and protease. Among the mixtures of SAP and several antacids, magnesium oxide-SAP showed the highest proteolytic activity.

• Journal of Pharmaceutical Investigation
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• v.18 no.3
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• pp.125-131
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• 1988

This study was undertaken to investigate the proteolytic enzyme from Neungee mushroom [Sarcodon aspratus (Berk) S. Ito]. The proteolytic activity of Neungee was higher than other several edible mushrooms under various pHs. The potency of proteolytic enzyme of Neungee was same as the digestive drugs containing protease. So the proteolytic activity of the enzyme was increased in neutral or weak alkaline pH, whose characteristics would be alkaline protease. The specific activity of the purified enzyme obtained by using Tris acryl CM-cellulose ion exchange increased 20 times as compared with that of the crude extract. The proteolytic enzyme was stable at room temperature, but decomposition was fast when incubated at higher temperature more than $40^{\circ}C$. The half life of the enzyme was longest in neutral pH and rate constant was increased in acidic or alkaline solution.

• The Korean Journal of Food And Nutrition
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• v.6 no.1
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• pp.1-7
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• 1993

19 Samples of koji-starters using in brewing were collected from Korea and Japan, and then 31 strains of koji-molds were isolated from them. After Identification of the Isolate, rice koji was made with each strains, and its saccharogenic activity, dextrogenic activity, proteolytic activity, acid Producing ability, browning reaction and flavor were tested. Among 31 strains of isolates, 10 strains were Identified as Asp nwamori var. kawachii, 18 strains as Asp. oryzae, 3 strains as Asp. usamii mkt. shirousamii. The koji-starters made in Korea were composed of single species of koji-mold with same strain, but those made in Japan were composed of the mixture of different two species or the mixture of different 2 ∼4 strains in same species. Judging from amylolytic and proteolytic ability by species, Asp. awamori var. kawachii H1, I1 and 11, Asp. owsae J2, L2, M2, P3 and P4, and Asp. usamii writ. shirousamii S1 were better than the others. Mold strains isolated from Korean koji-starters were much lower in amylolytic or proteolytic activity than those from Japanese koji-starters. The typical characteristics for the 3 species of koji-molds were that Asp. awamori var. kawachii was strong in acid producing ability, but week in amylolytic and proteolytic ability, that Asp. owzae had strong amylolytic activity and good aroma, but produced little amount of acid, and that Asp. usamii mut. shirousamii had strong Proteolytic activity but some off-flavor.

• Microbiology and Biotechnology Letters
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• v.1 no.2
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• pp.99-104
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• 1973

A study on the active center of the acid protease from Penicillium sp. was conducted, and also the milk clotting activity of acid prorease was measured. 1. PCMB failed to influence the proteolytic activity of acid protease, indicating that a reactive sulfhydryl group is not required for the enzymatic activity. 2. $\varepsilon$-amino caproic acid did not show any inhibitory effect on tile proteolytic activity of acid protease. 3. Also 2, 4-dinitro phenol did not show any inhibitory effect on the enzyme activity. 4. Acid protease from Penicillium sp. showed a strong milk clotting activity in the presence of Ca ion. 5. This enzyme had a strong proteolytic activity on various substrate, such as casein, denatured hemoglobin, ovalbumin, denatured bovine muscle protein, denatured percine muscle protein and denatured chicken muscle protein.

• Microbiology and Biotechnology Letters
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• v.37 no.3
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• pp.183-188
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• 2009

Seven isolates showing strong proteolytic activity, KYC 1028, 1100, 1134, 1139, 1151, 1159, and 1182, were collected. Out of them, the broth of KYC 1134 and KYC 1139 showed the high proteolytic activity measured by azocazein. To determine 16S rDNA sequences for identification, 16S rDNA of seven isolates were amplified and compared with the 16S rDNA sequences of other myxobacteria at NCBI. It is evident from the phylo-genetic tree that the isolates belong to the genus Myxococcus. Sharing high percentage similarity values with myxobacteria, the 16S rDNA sequences were involved in two species, Myxococcus macrospores and M. Fulvus. Biochemical characteristics of KYC 1134 broth, which showed the highest proteolytic activity, showed increased activity 8 times to seven days after culture, and protein production were increased gradually and stopped at five days. The broth had optimal temperature at $60^{\circ}C$ for proteolytic activity, and stability of pH was ranged from pH 5 to 10, at $50^{\circ}C$ and 60, respectively. To classify proteases being in the broth, ten inhibitors were determined and only bestatin showed 27% inhibition effect. The inhibition result demonstrates that the broth contains kinds of amino peptidases and other exopeptidases.

• Journal of Life Science
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• v.10 no.2
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• pp.218-227
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• 2000

Bone morphogenetic protein 1 (BMP-1) is part of a complex capable of inducing ectopic bone formation in mammals. Studies on TGF-β1 processing and Drosophila dorsal-ventral patterning have focused attention on BMP-1 as important in mediating the biological activity of this bone inducing complex. Herein, the bacterial expression, refolding, purification, and initial characterization of the BMP-1 proteolytic domain (BPD) are described. A semi-quantitative fluorescence-based thin layer chromatography assay was developed to assist in rapidly screening for optimal renaturation conditions. According to a preliminary screen for optimal conditions for the refolding of BPD , a detectable proteolytic activity against a high turnover substrate for astacin, a homologous protease from crayfish was observed. The conditions identified have allowed the expression of sufficient amounts of BPD for the characterization of the protein. Its proteolytic activity exhibits the same cleavage specificity as astacin against seven substrates that were previously synthesized for studying astacin. Furthermore, this activity is inhibited by the metal chelator 1,10-phenanthroline but not by its analogue 1,7-phenanthroline. The collagenase inhibitor Pro-Leu-Gly hydroxamate was found to inhibit both astacin and BPD activity. The results presented in this paper argue that BMP-1 does in fact possess an intrinsic proteolytic activity.

• Culinary science and hospitality research
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• v.11 no.2
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• pp.110-124
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• 2005

This study was conducted to investigate the proteolytic properties of Sarcodon aspratus on meat proteins. The analytical condition for the measurement of enzyme activity was determined and the effect of Sarcodon aspratus on beef protein and its fractions were determined by SDS-PAGE and the spectrophotometric method respectively. Optimum temperature and pH of Sarcodon aspratus were $73~78^{\circ}C$ and pH 8 respectively. However, enzyme tended to be denatured at $50^{\circ}C$ for 10 min incubation. Proteolytic activity of Sarcodon aspratus was higher than of kiwi and pear 66 and 990 times by dry weight respectively. It appeared that proteolytic activity of Sarcodon aspratus toward beef protein by SDS-PAGE was prominent when compared to that of kiwi and bromelain. Furthermore, Sarcodon aspratus showed the highest proteolytic activity toward all the beef protein fractions, which was followed by collagenase and bovine protease. Transmission electron microscopy showed the muscle fiber started to be degraded when treated with Sarcodon aspratus(1,000 unit) for 10min at $25^{\circ}C$. No distinct sarcomere, A-band, or z-line was observed when treated with Sarcodon aspratus for 60min at the same condition.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.576-579
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• 1998

Water extract of mulberry tree barks(Morus alba Linne) was studied for its proteolytic activity. Protein content of the extract was 1.12mg/ml and its specific activity was 5.14U/ml. The enzyme was active on various proteins : the relative acitities were 100 for casein, 63 for albumin, 58 for collagen, 45 for hemoglobin and 36 gelatin, respectively. There suggested that the ability of the enzyme to hydrolyze meat was relatively high since those are major meat proteins. Optimum pH and temperature for proteolytic activity were : pH 6.0 and 6$0^{\circ}C$. And the enzyme was stable at the pH range of 6.0 to 7.0 and temperature between 50 and 8$0^{\circ}C$. Apparent proteolytic activities could support some scientific grounds of traditional application of mulberry tree barks to home cooking for meat tenderization.

• Korean Journal of Microbiology
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• v.18 no.1
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• pp.15-19
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• 1980

In order to study on the pigment and protease of Serratia marcescens, the correlation between protease activity and pigment formation was investigated. The results are as follows ; (1) The protease activity exhibitied two pH optima 6.0 and 7.5, respectively. (2) The optimal temeprature of proteolytic activity was $45^{\circ}C$. With these-results, it is suggested that the proteolytic enzymes of Serratia masrecescens is stable at neutral pH range and more active at the high temeprature than lthat of otehr proteolytic enzymes.