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EFFECT OF EUGLENA FEEDING ON THE CONTENT OF TAURINE IN THE MEAT OF BROILER CHICKENS
ENOMOTO, TOSHIKI,HAYASHI, MASAHIRO,MIYATAKE, KAZUTAKA,NAKANO, YOSHIHISA,PAIK, IN-KEE,PARK, BONG-SUN 중앙대학교 식량자원연구소 2000 食糧資源硏究所 論文集 Vol.12 No.1
Broiler chickens just after hatching were fed diets supplemented with Euglena cells for one month. The following groups (each 30 boiler chickens) were used group 1, fed the control diet, group 2, fed Euglena making up 0 25% of the diet; group 3, fed Euglena making up 0.50% of the diet. group 4. fed Euglena making up 1.00% of the diet. All groups fed Euglena grew satisfactorily as well as the control during the experimental periods. Although Euglena did not contain taurine at all, taurine content of the muscle in the Euglena groups increased about 2~3 tomes in comparison with the control. From these results. the effect of Euglena feeding for broiler chickens and the accumulation mechanism of taurine in the muscle are discussed.
Effect of trehalose and trehalase production for mycelium growth of Tricholoma matsutake
Mizuho Kusuda,Ryosuke Yodono,Mitsuhiro Ueda,Norifumi Shirasaka,Kazutaka Miyatake,Takao Terashita 한국버섯학회 2010 한국버섯학회지 Vol.8 No.4
Effect of trehalose for the mycelial growth of Tricholoma matsutake were examined. When T. matsutake Z-1 strain was cultured in the partially modified matsutake liquid (PMML) medium and the Hamada matsutake liquid (HML) medium supplemented with trehalose at 24 ℃ for 80days, the vegetative mycelial dry weights showed higher value compared with those of PMML medium and HML medium supplemented with glucose (control). The range of the effect of 1.0-8.0% carbohydrate substrate on vegetative mycelial growth was investigated. The optimal concentration for mycelial growth was 2.0% for the glucose medium but 8.0% for the trehalose medium. To evaluate the potential of the production of trehalase from T. matsutake, the extracellular trehalase activity during the vegetative mycelial growth was measured. The activity of the extracellular trehalase increased during vegetative mycelial growth of T. matsutake and was maximal 70 days after inoculation. This extracellular enzyme was investigated for the purification and the characterization. The partially purified trehalase was obtained from about 1.53l static culture filtrate, with 19.1% recovery, and about 2,940 fold purification. The molecular mass was about 62.6kDa (SDS-PAGE) and 70kDa (Gel-filtration). The enzyme was most active around 40℃ and pH 5.0 and stable over a pH of 4.5~ 6.5 for 30min at 37℃. The enzyme readily hydrolyzed trehalose having α -1,1 glucosidic bond. However, it did not hydrolyze disaccharides such as maltose, iso-maltose, cellobiose, saccharose and lactose.
Purification, characterization and gene cloning of metalloprotease from Nomuraea atypicola
Naomi Yamamoto,Mitsuhiro Ueda,Mizuho Kusuda,Masami Nakazwa,Kenji Ohuchi,Minoru Sakaguchi,Kuniyo Inouye,Kazutaka Miyatake 한국버섯학회 2010 한국버섯학회지 Vol.8 No.4
We have purified and characterized of metalloprotease metalloprotease from Nomuraea atypicola. N. atypicola was cultured in Sabouraud medium supplemented with powdered pupae. The metalloprotease from culture supernatant was purified to electrophoretically homogeneous state. The molecular mass of metalloprotease from N. atypicola was 50 kDa. The enzyme was most active at pH 8.5 and 40oC and stable at pH 5.0-7.0 and up to 40oC. The activity was inhibited by o-phenanthroline and EDTA. The N-terminal amino acid sequence of the enzyme showed a similarity to those of proteases (Metallo peptidase M36 family (Fungalysin)) from Coccidioides posadasii and Aspergillus fumigatus. The enzyme was found to be Fungalysin-like metalloprotease. cDNA encoding metalloprotease from N. atypicola was amplified by PCR using oligonucleotides deduced from the N-terminal endo peptide sequence, 5’- and 3’-RACE. Predicted enzyme structure consists of 637 amino acids with pro- and signal sequences. The mature enzyme had 391 amino acids and its deduced amino acid sequence coincided completely with the N- terminal amino end (20 amino acids) of metalloprotease purified from N. atypicola. We are studying on expression of the metalloprotease gene in Escherichia coli.