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Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus
Park, Pyo-Jam,Lee, Sang-Hoon,Byun, Hee-Guk,Kim, Soo-Hyun,Kim, Se-Kwon 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.6
Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.5 and $55^{\circ}C$, respectively. The $K_m$ and $V_{max}$ of the enzyme for collagen Type I were approximately 1.1 mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by $Hg^{2+}$, $Zn^{2+}$, PMSF, TLCK, and the soybean-trypsin inhibitor.
Park, Pyo-Jam,Kim, Eun-Kyung,Lee, Seung-Jae,Park, Sun-Young,Kang, Dong-Soo,Jung, Bok-Mi,Kim, Kui-Shik,Je, Jae-Young,Ahn, Chang-Bum The Korean Society of Food Science and Nutrition 2009 Journal of medicinal food Vol.12 No.1
Enzymatic hydrolysates of Laminaria japonica were evaluated for antioxidative activities using hydroxyl radical scavenging activity and protective effects against $H_2O_2$-induced DNA and cell damage. In addition, activities of antioxidative enzymes, including catalase, glutathione peroxidase, and glutathione S-transferase, of the enzymatic hydrolysates from L. japonica were also estimated. L. japonica was first enzymatically hydrolyzed by seven carbohydrases ($Dextrozyme^{(R)}$, $AMG^{(R)}$, $Promozyme^{(R)}$, $Maltogenase^{(R)}$, $Termamyl^{(R)}$, $Viscozyme^{(R)}$, and $Celluclast^{(R)}$ [all from Novo Co., Novozyme Nordisk, Bagsvaerd, Denmark]) and five proteinases ($Flavourzyme^{(R)}$, $Neutrase^{(R)}$, $Protamex^{(R)}$, $Alcalase^{(R)}$ [all from Novo Co.], and pancreatic trypsin). The hydroxyl radical scavenging activities of Promozyme and pancreatic trypsin hydrolysates from L. japonica were the highest as compared to those of the other carbohydrases and proteinases, and their 50% inhibitory concentration values were 1.67 and $317.49\;{\mu}g/mL$, respectively. The pancreatic trypsin hydrolysates of L. japonica exerted a protective effect on $H_2O_2$-induced DNA damage. We also evaluated the protective effect on hydroxyl radical-induced oxidative damage in PC12 cells via propidium iodide staining using a flow cytometer. The AMG and pancreatic trypsin hydrolysates of L. japonica dose-dependently protected PC12 cells against cell death caused by hydroxyl radical-induced oxidative damage. Additionally, we analyzed the activity of antioxidative enzymes such as catalase, glutathione peroxidase, and the phase II biotransformation enzyme glutathione S-transferase in L. japonica-treated cells. The activity of all antioxidative enzymes was higher in L. japonica-treated cells compared with the nontreated cells. These results indicate that enzymatic hydrolysates of L. japonica possess antioxidative activity.
Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus
( Pyo Jam Park ),( Sang Hoon Lee ),( Hee Guk Byun ),( Seo Hyun Kim ),( Se Kwon Kim ) 생화학분자생물학회 2002 BMB Reports Vol.35 No.6
Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.5 and 55℃, respectively. The K_m and V_max of the enzyme for collagen Type I were approximately 1.1 mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by Hg^2+, Zn^2+, PMSF, TLCK, and the soybean-trypsin inhibitor.