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微信小章| 产品名称： | Aspergillus phoenicis (Corda) Thom |
|---|---|
| 商品货号： | TS210058 |
| Deposited As： | Aspergillus saitoi Sakaguchi et al., anamorph |
| Strain Designations： | R3813 Black Aspergillus 2 |
| Application： | produces acid carboxypeptidase produces acid protease protease (acid) produces glutaminase produces mannosidase, alpha Man9-mannosidase, mannosidase, alpha produces glutaminase for flavor-enhancing of foods |
| Biosafety Level： | 1
Biosafety classification is based on U.S. Public Health Service Guidelines, it is the responsibility of the customer to ensure that their facilities comply with biosafety regulations for their own country. |
| Product Format： | freeze-dried |
| Type Strain： | no |
| Disclosure： | This material is cited in a US or other Patent and may not be used to infringe the claims. Depending on the wishes of the Depositor, ATCC may be required to inform the Patent Depositor of the party to which the material was furnished. This material may not have been produced or characterized by ATCC. |
| Preceptrol®： | no |
| Medium： | ATCC® Medium 336: Potato dextrose agar (PDA) |
| Growth Conditions： | Temperature: 24.0°C |
| Name of Depositor： | Noda Inst. Sci. Res. |
| U.S. Patent Number： | |
| Cross References： | Nucleotide (GenBank) : D25318 aspergillopepsin I gene, complete coding sequence Nucleotide (GenBank) : D49827 1,2-alpha-D-mannosidase gene, msdS, complete coding sequence |
| References： | Tanaka N, et al. Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity. Biochim. Biophys. Acta 485: 406-416, 1977. PubMed: 21699 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 |