• Journal of Microbiology and Biotechnology
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• v.30 no.8
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• pp.1116-1123
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• 2020

Velvet antler (VA) is a historically traditional medicinal supplement and is well known in Asian countries for its pharmaceutical and health benefits. The objectives for this study were to optimize the hot water extraction (HWE) of VA for the Korean VA industry, and to determine the most effective pretreatment method among microwave (MW), ultrasonication (US), and enzymatic (EZ) techniques. Using response surface methodology, optimum extraction temperatures and times were determined by central composite design configuration based on extraction yield and sialic acid content. Various quality parameters of VA extract including yield, soluble solid, protein, and sialic acid contents were also compared with the conjunction of HWE and pretreatment. The yield and sialic acid content of VA extract were determined to be 40% and 0.73 mg/g, respectively, under an optimum temperature of 100℃ at 24 h of extraction time. The yields from VA extracts pretreated with MW, US, and EZ were 17.42%, 19.73%, and 29.15%, respectively. Among the tested commercial enzymes, pepsin was the most effective proteolytic enzyme and led to the highest yield (47.65%), soluble solids (4.03 °brix), protein (1.12 mg/ml), and sialic acid (3.04 mg/ml) contents from VA extract.

• Asian Pacific Journal of Cancer Prevention
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• v.15 no.3
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• pp.1085-1091
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• 2014

Matrix metalloproteinases (MMPs) are a family of zinc dependent extracellular matrix (ECM) remodelling endopeptidases having the ability to degrade almost all components of extracellular matrix and implicated in various physiological as well as pathological processes. Carcinogenesis is a multistage process in which alteration of the microenvironment is required for conversion of normal tissue to a tumour. Extracellular matrix remodelling proteinases such as MMPs are principal mediators of alterations observed in the microenvironment during carcinogenesis and according to recent concepts not only have roles in invasion or late stages of cancer but also in regulating initial steps of carcinogenesis in a favourable or unfavourable manner. Establishment of relationships between MMP overproduction and cancer progression has stimulated the development of inhibitors that block proteolytic activity of these enzymes. In this review we discuss the MMP general structure, classification, regulation roles in relation to hallmarks of cancer and as targets for therapeutic intervention.

• Proceedings of the Korean Society of Applied Pharmacology
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• 2003.11a
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• pp.84-84
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• 2003

Lead has long been considered as a toxic environmental pollutant, which severely damages central nervous system. Lead can cause hypo- and de-myelination, and glial cells are closely related with myelination or demyelination. Matrix metalloproteinases (MMPs) are proteolytic enzymes that are involved in the remodelling of the extracellular matrix in a variety of physiological and pathological processes. MMPs also seem to be important in the pathogenesis of inflammatory demyelinating diseases of the central and peripheral nervous system. In this study, we investigated whether lead affects MMP-9 expression in rat primary glial cells. Treatment of 0.1-5 ${\mu}$M lead dose- and time-dependently increased MMP-9 expression in rat primary glial cells. The activity of MMPs was determined using zymography. Lead activated Erk(1/2) but neither of the other endogenous MAP kinases, p38 or JNK. Inhibition of Erk(1/2) activation by PD98059, a MEK inihibitor, prevented lead-induced expression of MMP-9. The results of the present study suggest that lead intoxication may adversely affect brain function at least in part by inducing MMP-9 expression through Erk(1/2) activation in primary glial cells.

• Food Science of Animal Resources
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• v.40 no.3
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• pp.415-425
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• 2020

It is believed that two main proteolytic systems are involved in the tenderization of meat: the cathepsins and the calpains. Many researchers consider the calpain system to be the major contributor to meat tenderness during post-mortem storage. However, the role and activity of cathepsins during post-mortem storage or low temperature meat processing is unclear, particularly for the tough meat cuts like brisket. Thus, the study was designed to investigate the effects of cold (refrigerated and frozen) storage and sous vide processing on the activities of cathepsin B, H, and L in beef brisket. There were no significant changes in pH and cathepsin H activity throughout the 18 d of storage at both temperatures. However, an increase in cathepsin B activity was observed during the first 4 d at both storage temperatures, but subsequently the activity remained unchanged. Cathepsins B and L were found to be more heat stable at sous vide temperatures (50℃ for 24 h, 55℃ for 5 h and at 60℃ and 70℃ for 1 h) compared to cathepsin H. Cathepsin B+L activity was found to increase after sous vide cooking at 50℃ for 1 h but decreased to about 47% relative to the uncooked control after 24 h of cooking. These results suggest that cathepsins B and L may contribute to the improved meat tenderness usually seen in sous vide cooked brisket meat.

• Archives of Pharmacal Research
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• v.21 no.3
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• pp.260-265
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• 1998

Angiogenic activity of Aloe vera gel was investigated by in vitro assay. We obtained the most active fraction from dichloromethane extract of Aloe vera gel by partitioning between hexane and 90% aqueous methanol. The most active fraction (F3) increased the proliferation of calf pulmonary artery endothelial (CPAE) cells. In addition, F3 fraction induced CPAE cells to invade type I collagen gel and form capillary-like tube through in vitro angiogenesis assay, and increased the invasion of CPAE cells into matrigel through in vitro invasion assay. Furthermore, the effect on the MRNA expression of proteolytic enzymes which are key participants in the regulation of extracellular matrix degradation was investigated by northern blot analysis. F3 fraction enhanced mRNA expression of urokinase-type plasminogen activator (u-PA), matrix metalloproteinase-2 (MMP-2), and membrane-type MMP (MT-MMP) in CPAE cells whereas the expression of plasminogen activator inhibitory (PAl-1) mRNA was not changed.

• BMB Reports
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• v.29 no.5
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• pp.484-487
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• 1996

The matrix metalloproteinases (MMPs) are members of a unique family of proteolytic enzymes that degrade components of the extracellular matrix. Significant evidence has accumulated to directly implicate members of the MMPs in tumor invasion and metastasis formation. To investigate the correlation between ras oncogene and MMP gene expression in various tumor cells, we detected mRNAs for the ras, MMP-2 and MMP-9 (72 kD and 92 kD type IV collagenases, respectively) genes in nine human tumor cell lines. The ras gene was expressed in seven cell lines; MMP-2 in three; MMP-9 in two cell lines tested. There was no direct correlation between the ras oncogene and MMP expression. A clear difference in the mRNA expression between MMP-2 and MMP-9 was observed among the cell lines. As an approach to study the effect of the ras oncogene on metastasis, we examined the expressions of MMP-2 and MMP-9 in HT1080 cells transfected with the v-H-ras gene. MMP-9 expression was Significantly enhanced in the ras-transfected HT1080 cells compared with the nontransfectants while ras transfection did not affect the expression of MMP-2. These results suggest the possible inducing effect of the ras oncogene on the metastasis by activation of the MMP-9 gene in HT1080.

• Preventive Nutrition and Food Science
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• v.11 no.2
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• pp.120-126
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• 2006

Fish backbone, a major by-product in the fish processing industry, accounts for about 15% of whole fish weight. In this study, recovery of bioavailable calcium from Alaska pollack (Theragra chalcogramma) backbone by-products using enzymatic hydrolysis was investigated. Finely ground fish backbones were hydrolyzed with two proteolytic enzymes (pepsin and protease) to obtain soluble calcium from the by-products. The pepsin digest had a higher degradation efficiency (88%) than protease. Four different concentrations of the fish backbone calcium (100, 250, 500 and 1000 mg/L) prepared by the pepsin digest were treated with $Na_2HPO_4$ at a concentration gradient (0, 1, 2, 4, 8, 10, 15 and 20 mM) to evaluate their solubility, revealing that solubilities of the fish backbone calcium were superior to those of $CaCl_2$ at all the calcium and $Na_2HPO_4$ concentrations. Among the tested concentrations the highest solubility was found in the pepsin digest containing a calcium concentration of 1000 mg/L. Thus, hydrolyzing with pepsin is an effective mode of recovering bioavailable calcium from Alaska pollack fish backbones.

• Journal of Microbiology and Biotechnology
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• v.1 no.2
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• pp.96-101
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• 1991

Phenotypic changes after plasmid curing experiment suggested that the bacteriocin production phenotype ($Bac^{+}$) might be linked to a chromosomal DNA and the mucin production phenotype ($Muc^{+}$) might be linked to a 62.5 kilobase (kb) plasmid (pMUC62) in Lactobacillus plantarum 27 isolated from meat starter culture. The non-mucoid ($Muc^{-}$) variants were missing pMUC62 but they produced bacteriocin as the wild strain ($Bac^{+}$). There was no difference in antibiotic resistance and sugar fermentation patterns between the wild strain ($Bac^{+}$ $Muc^{+}$) and the nonmucoid ($Bac^{+}$ $Muc^{-}$) variants. Antimicrobial spectrum of bacteriocin produced by both wild strain and $Muc^{-}$ variant of Lb. plantarum 27 included strains of Pediococcus acidilactici (A, M, H), Pediococcus sp. isolated from meat, Lactobacillus sp. isolated from meat, Lb. plantarum NCDO 955 and Staphylococcus aureus 485. Neither of the tested Gram negative bacteria were inhibited by bacteriocin. Antimicrobial activity of crude bacteriocin was retained after autoclaving, DNase or catalase treatment and exposure from pHs 4 to 9 but was lost after treating with several proteolytic enzymes and exposure at pH 10.

• Korean Journal Plant Pathology
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• v.14 no.5
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• pp.376-381
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• 1998

Xanthomonas campestris pv. glycines 8ra causes bacterial pustule disease on susceptible soybean leaves and produces a bacteriocin, named glycinecin, against related bacteria such as Xanthomonas campestris pv. vesicatoria. The antimicrobial activity of the glycinecin was effective to most tested Xanthomonas species. X. c. pv. glycines 8ra was able to produce the glycinecin in liquid media as well as solid media. Maximal productivity of glycinecin was obtained at 3$0^{\circ}C$ in the early stationary phase of growth of the X. c. pv. glycines 8ra. The production of glycinecin was not dependent on the initial inoculum level but on cell density. Glycinecin was very sensitive to proteolytic enzymes such as trypsin and proteinase K but resistant to DNase and RNase. The culture supernatant of X. c. pv. glycines 8ra retained some of its antimicrobial activity after 15 min at 6$0^{\circ}C$. It is stable at wide range of pH. The glycinecin showed the bactericidal activity after the adsorption of the glycinecin to the sensitive bacterial cell.

• Textile Coloration and Finishing
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• v.17 no.6 s.85
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• pp.51-59
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• 2005

To manufacture hightech easycare wool, there are several methods which use strong oxidising agent or the resin treatment, however, neither are environmentally friendly methods. Moreover it may deteriorate the handle. The aim of this study is to manufacture the hightech easycare wool using the modified Fenton method which can be formed by hydrogen peroxide and ferric sulfate and enzyme treatment. The method was pretreated by ferric sulfate on the wool surface and then the surface of wool scale was selectively removed by ferric ion catalyst. Subsequently the Enchiron which is one of the proteolytic enzymes was treated on the wool surface. The treated wool had the result of having optimum weight loss and excellent whiteness and good handle. Therefore implications of these results suggest that this method using the modified Fenton method and enzyme treatment may be one way of manufacturing the hightech easycare wool.