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ATCC14332

ZKCC-45321

ATCC14332

价格
¥3,200

所有产品仅供生命科学研究使用,不可用于临床与治疗。

Description

产品说明

所属分类微生物 > 模式菌株
品牌 / 来源CS-BIC | 中科生信
应用科研,生产,主要用于产生酸性羧肽酶,生产酸性蛋白酶(酸),产生谷氨酰胺酶,产生甘露糖苷酶,α-man9甘露糖苷酶,甘露糖苷酶,α,生产谷氨酰胺酶提高食品风味
培养基ATCC® Medium 336: Potato dextrose agar (PDA)
存储人Noda Inst. Sci. Res.
出品公司ATCC
参考文献Ichishima E, et al. Purification of an acidic alpha-D-mannosidase from Aspergillus saitoi and specific cleavage of 1,2-alpha-D-mannosidic linkage in yeast mannan. Biochim. Biophys. Acta 658: 45-53, 1981. PubMed: 7011404 Yokotsuka T, et al. Hydrolysis of glutamine within foods and beverages to glutamic acid. US Patent 3,717,470 dated Feb 20 1973 Yoshida F, Ichishima E. Method of producing a proteolytic enzyme by use of black Aspergillus type molds. US Patent 3,149,051 dated Sep 15 1964 Chiba Y, et al. The carbohydrate moiety of the acid carboxypeptidase from Aspergillus saitoi. Curr. Microbiol. 27: 281-288, 1993. PubMed: 7764137 Shintani T, Ichishima E. Primary structure of aspergillopepsin I deduced from nucleotide sequence of the gene and aspartic acid-76 is an essential active site of the enzyme for trypsinogen activation. Biochim. Biophys. Acta 1204: 257-264, 1994. PubMed: 8142467 Inoue T, et al. Molecular cloning and nucleotide sequence of the 1,2-alpha-D- mannosidase gene, msdS, from Aspergillus saitoi and expression of the gene in yeast cells. Biochim. Biophys. Acta 1253: 141-145, 1995. PubMed: 8519794 Ichishima E, et al. Studies on the proteolytic enzymes of black aspergilli. Effect of agitation and aeration on submerged production of acid protease. Rep. Noda Inst. Sci. Res. 7: 1-8, 1963. Takeuchi M, Ichishima E. Improved purification and further characterization of acid carboxypeptidase from Aspergillus saitoi. Agric. Biol. Chem. 50: 1403-1407, 1986. Ichishima E, et al. Production of a new type of acid carboxypeptidase of molds of the Aspergillus niger group. Appl. Microbiol. 26: 327-331, 1973. PubMed: 4796163 Ichishima E. Purification and characterization of a new type of acid carboxypeptidase from Aspergillus. Biochim. Biophys. Acta 258: 274-288, 1972. PubMed: 4621676
模式菌株否
生长条件24 ℃
菌株特点ATCC 14332是海枣曲霉,Aspergillus phoenicis 。Nucleotide (GenBank) : D25318 aspergillopepsin I gene, complete coding sequence Nucleotide (GenBank) : D49827 1,2-alpha-D-mannosidase gene, msdS, complete coding sequence
菌株类型海枣曲霉,Aspergillus phoenicis
菌种又名R3813 [Black Aspergillus 2]
菌种名称ATCC14332, ATCC 14332
产品目录号14332
生物安全等级1
其他保藏库编号BCRC33856,ATCC 14332
ATCC14332标准菌株基本信息ATCC
ATCC14332, ATCC 14332
R3813 [Black Aspergillus 2]
海枣曲霉,Aspergillus phoenicis
Noda Inst. Sci. Res.
14332
BCRC33856,ATCC 14332
ATCC® Medium 336: Potato dextrose agar (PDA)
24 ℃
1
否
科研,生产,主要用于产生酸性羧肽酶,生产酸性蛋白酶(酸),产生谷氨酰胺酶,产生甘露糖苷酶,α-man9甘露糖苷酶,甘露糖苷酶,α,生产谷氨酰胺酶提高食品风味
ATCC 14332是海枣曲霉,Aspergillus phoenicis 。Nucleotide (GenBank) : D25318 aspergillopepsin I gene, complete coding sequence
Nucleotide (GenBank) : D49827 1,2-alpha-D-mannosidase gene, msdS, complete coding sequence
Ichishima E, et al. Purification of an acidic alpha-D-mannosidase from Aspergillus saitoi and specific cleavage of 1,2-alpha-D-mannosidic linkage in yeast mannan. Biochim. Biophys. Acta 658: 45-53, 1981. PubMed: 7011404
Yokotsuka T, et al. Hydrolysis of glutamine within foods and beverages to glutamic acid. US Patent 3,717,470 dated Feb 20 1973
Yoshida F, Ichishima E. Method of producing a proteolytic enzyme by use of black Aspergillus type molds. US Patent 3,149,051 dated Sep 15 1964
Chiba Y, et al. The carbohydrate moiety of the acid carboxypeptidase from Aspergillus saitoi. Curr. Microbiol. 27: 281-288, 1993. PubMed: 7764137
Shintani T, Ichishima E. Primary structure of aspergillopepsin I deduced from nucleotide sequence of the gene and aspartic acid-76 is an essential active site of the enzyme for trypsinogen activation. Biochim. Biophys. Acta 1204: 257-264, 1994. PubMed: 8142467
Inoue T, et al. Molecular cloning and nucleotide sequence of the 1,2-alpha-D- mannosidase gene, msdS, from Aspergillus saitoi and expression of the gene in yeast cells. Biochim. Biophys. Acta 1253: 141-145, 1995. PubMed: 8519794
Ichishima E, et al. Studies on the proteolytic enzymes of black aspergilli. Effect of agitation and aeration on submerged production of acid protease. Rep. Noda Inst. Sci. Res. 7: 1-8, 1963.
Takeuchi M, Ichishima E. Improved purification and further characterization of acid carboxypeptidase from Aspergillus saitoi. Agric. Biol. Chem. 50: 1403-1407, 1986.
Ichishima E, et al. Production of a new type of acid carboxypeptidase of molds of the Aspergillus niger group. Appl. Microbiol. 26: 327-331, 1973. PubMed: 4796163
Ichishima E. Purification and characterization of a new type of acid carboxypeptidase from Aspergillus. Biochim. Biophys. Acta 258: 274-288, 1972. PubMed: 4621676

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