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Aspergillus phoenicis (Corda) Thom
Aspergillus phoenicis (Corda) Thom
規(guī)格:
價(jià)格:詢價(jià)
編號(hào):B166549
品牌:Mingzhoubio

標(biāo)準(zhǔn)菌株
定量菌液
DNA
RNA

規(guī)格:
凍干粉
斜面
甘油
平板


產(chǎn)品名稱
Aspergillus phoenicis (Corda) Thom
商品貨號(hào)
B166549
Deposited As
Aspergillus saitoi Sakaguchi et al., anamorph
Strain Designations
R3813 [Black Aspergillus 2]
培養(yǎng)基
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

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