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The Degradation of Chitin with Food Grade Papain
(Beom Ku Han,(Tak You,(Jong Kook Moon,(Sae Bom Kim,(Do Hyun Jo 한국응용생명화학회 2000 Journal of Applied Biological Chemistry (J. Appl. Vol.43 No.4
We investigated the production of chitin oligosaccharides using food grade papain. A solution of commercial food grade papain (FGP) was dialyzed for 12 h before measuring its chitinolytic activity. The effects of enzyme concentration, reaction temperature
The Degradation of Chitin with Food Grade Papain
Han, Beom-Ku,You, Tak,Moon, Jong-Kook,Kim, Sae-Bom,Jo, Do-Hyun 한국응용생명화학회 2000 Journal of Applied Biological Chemistry (J. Appl. Vol.43 No.4
We investigated the production of chitin oligosaccharides using food grade papain. A solution of commercial food grade papain (FGP) was dialyzed for 12 h before measuring its chitinolytic activity. The effects of enzyme concentration, reaction temperature, and pH on the endochitinase and $\beta$-N-acetylglucosaminidase activities and the thermostability of these enzymes were investigated. In adddition, the reaction products were analyzed with gel filtration on a Bio-Gel P2. The endochitinase activity was twentyfold higher than that of $\beta$-N-acetylglucosaminidase. The optimal endochitinase activity was at pH 3.0, while the maximal $\beta$-N-acetylglucosaminidase activity was at pH 6.0. The reaction product consisted mainly of the dimer of N -acetylglucosamine, with a small amount of its trimer. Under the experimental conditions, $120{\mu}g$ of chitin oligomers were obtained with 1 mg of FGP protein after an incubation of 2 h.
Purification and Characterization of Acidic Chitinases from Gizzards of Broiler ( Gallus gallus L. )
(Beom Ku Han),(Jong Kook Moon),(Yeon Woo Ryu),(Yun Hee Park),(Do Hyun Jo) 생화학분자생물학회 2000 BMB Reports Vol.33 No.4
Acidic chitinases from the gizzards of a broiler were purified to homogeneity, using precipitation with (NH₄)₂SO₄, ion exchanger chromatography, gel filtration, chromatofocusing and hydrophobic interaction chromatography The enzymes, GAC1 and GAC2, were purified 180- and 194folds with a recovery of 4.9% and 2.7%, respectively The molecular mass of GAC1 and GAC2 were 48.2 kDa and 57.8 kDa, respectively Chromatofocusing resulted in a pI of 3.1 for both enzymes. The purified enzymes were endochitinases that were devoid of β-N-acetylglucosaminidase and lysozyme activity. Kinetic studies using [³H]chitin indicate that GAC1 has a K_m and V_(max) of 1.97 ㎎/㎖ and 185 ㎎/㎎ protein/h, respectively The GAC2 has a K_m, and V_(max) of 0.42 ㎎/㎖ and 92.3 ㎎/㎎ protein/h, respectively at optimal pH and temperature (pH 5.0 and 60℃). When the pentamer and hexamer of Nacetylglucosamine (G1cNAc) were used as a substrate, the major product by GAC1 was the dieter of G1cNAc with a differential accumulation of the monomer and trimer, depending upon the substrate. However, the GAC2 produced the dieter and trimer in an equal quantity, regardless of the substrate used. The first 9 NH₂-terminal amino acid residues of the purified gizzard chitinase GAC1 and GAC2 shared a 100% homology. The first 25 NH₂-terminalamino acid residues of GAC1 also shared 55-60% homology with animal chitinasess and some animal proteins, such as whey protein and oviduct-specific proteins. However, little homology was found with either microbial and plant chitinases, or egg white lysozyme.
Purification and Characterization of Acidic Chitinases from Gizzards of Broiler (Gallus gallus L.)
Han, Beom-Ku,Moon, Jong-Kook,Ryu, Yeon-Woo,Park, Yun-Hee,Jo, Do-Hyun Korean Society for Biochemistry and Molecular Biol 2000 Journal of biochemistry and molecular biology Vol.33 No.4
Acidic chitinases from the gizzards of a broiler were purified to homogeneity, using precipitation with $(NH_{4})_{2}SO_{4}$, ion exchanger chromatography, gel filtration, chromatofocusing and hydrophobic interaction chromatography. The enzymes, GAC1 and GAC2, were purified 180- and 194- folds with a recovery of 4.9% and 2.7%, respectively. The molecular mass of GAC1 and GAC2 were 48.2 kDa and 57.8 kDa, respectively. Chromatofocusing resulted in a pI of 3.1 for both enzymes. The purified enzymes were endochitinases that were devoid of ${\beta}-N-acetylglucosaminidase$ and lysozyme activity. Kinetic studies using $[^3H]chitin$ indicate that GAC1 has a $K_m$ and $V_{max}$ of 1.97 mg/ml and 185 mg/mg protein/h, respectively. The GAC2 has a $K_m$ and $V_{max}$ of 0.42 mg/ml and 92.3 mg/mg protein/h, respectively at optimal pH and temperature (pH 5.0 and $60^{\circ}C$). When the pentamer and hexamer of N-acetylglucosamine (GlcNAc) were used as a substrate, the major product by GAC1 was the dimer of GlcNAc with a differential accumulation of the monomer and trimer, depending upon the substrate. However, the GAC2 produced the dimer and trimer in an equal quantity, regardless of the substrate used. The first 9 $NH_2-terminal$ amino acid residues of the purified gizzard chitinase GAC1 and GAC2 shared a 100% homology. The first 25 $NH_2-terminal$ amino acid residues of GAC1 also shared 55-60% homology with animal chitinases and some animal proteins, such as whey protein and oviduct-specific proteins. However, little homology was found with either microbial and plant chitinases, or egg white lysozyme.
한범구(Beom Ku Han),이우진(Woo Jin Lee),유탁(Tak You),박인호(In Ho Park),조도현(Do Hyun Jo) 한국응용생명화학회 1996 Applied Biological Chemistry (Appl Biol Chem) Vol.39 No.6
The survey on the chitinolytic activity of some plants was performed for the purpose of obtaining some reliable and inexpensive sources of chitinase. Rice, soybean for sprouting, kiwi fruit, almond and crude papain were investigated. Rice bran, seed coat of the soybean and the pericarp of kiwi fruit showed a considerable activity, while the bean after the removal of the seed coat, the mixture of rice integument and endosperm, polished rice, and defatted soybean powder didn`t have any detectable activity. These crude enzymes have shown to contain both endo- and exochitinase activity. The effects of pH and temperature on the enzyme activity were variable. Furthermore we have observed the chitosanolytic activity from these enzyme preparations. The rice bran had the highest activity in the enzymatic degradation of chitosan, and seed coat of soybean and the pericarp of kiwi fruit followed. On the basis of the fact that crude papain was not only commercially available but also the most potent in the endochitinase activity and the lowest in the exochitinase activity, we could conclude that crude papain was considered as the most suitable source of the chitinase among plants studied in this paper. In addition, rice bran was worth further investigation from the point of utilizing agricultural by-product.
쥐 뇌의 progesterone 대사에 미치는 연령의 효과
한범구(Beom Ku Han),박인호(In Ho Park),조도현(Do Hyun Jo) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.1
The effect of age on the metabolism of progesterone was studied in the rat brain. Metabolic activity was more active in minced tissues than total homogenates. The activity of progesterone 5α-reductase(s) was increased during postnatal periods(between 5 and 14 days after birth) and thereafter steadily decreased up to the one-fourth level of the fetus. When 5α-dihydroprogesterone was incubated with brain tissues of various ages, the change in the activity of 3α-hydroxysteroid oxidoreductase(3α-HSOR) was similar to that of 5α-reductase(s). These results suggest that the reduced formation of total 5α-reduced metabolites was due to the decreased activities of 5α-reductase(s) and 3α-HSOR. However the level of 3β-HSOR remained constant regardless of the age.
키토산의 효소분해산물로부터 수용성 올리고당의 분리 및 정제
한범구,이우진,조도현 한국키틴키토산학회 1998 한국키틴키토산학회지 Vol.3 No.3
Chitosan with 80% deaceylation and 30cps of viscosity was treated with papain, commercial chitosanase from Bacillus sp.(B-chitosanase), and a chitosanase from the digestive tract of broiler(G-chitosanase). Water-soluble chitosan oligomers were separated from the reaction mixture by differential precipitation and further analyzed by gel filteration. The conversion ratio of chitosan into water-soluble chitosan oligomers was 26% for B-chitosanase, 33% for G-chitosanase, and 39% for papain. With gel filteration of the separated oligomers, the major constituent was identified as dimer of glucosamine for B-chitosanase and papain and the trimer for G-chitosanase.