P2143
蛋白酶 来源于佐氏曲霉
Type XIII, ≥0.6 unit/mg solid
别名:
Molsin
应用
Aspergillus saitoi来源蛋白酶已用于一项评估大蛋白氢交换序列覆盖率和分辨率的研究中。它还被用于一项通过β-葡萄糖苷酶研究大豆凝乳异黄酮糖苷向其糖苷配基转化的研究中。
生化/生理作用
Aspergillus saitoi来源蛋白酶也可发挥β-葡萄糖苷酶的作用。
其他说明
在pH 2.8、37℃条件下，一单位每分钟可水解酪蛋白并产生相当于1.0 μ摩尔 (181 μg) 酪氨酸的显色（使用Folin-Ciocalteu试剂显色）。
警示用语：
Danger
危险分类
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
E Skyttä et al.
The Journal of applied bacteriology, 74(2), 134-142 (1993-02-01)
The broad-spectrum antibacterial activity exhibited by three Pediococcus strains isolated from beer was preliminarily characterized. Factors affecting the production rate of bacterial inhibitors were screened and the effects of simultaneous cultivation of Lactococcus and Pediococcus on the production of inhibitory
M E Kambouris et al.
FEMS immunology and medical microbiology, 25(3), 255-264 (1999-08-25)
In immunodeficient patients, Aspergillus species emerge as circumstantial pathogens. Aspergillus fumigatus is a distant first among the pathogenic aspergilli, which cause deep-seated mycoses. Sequences of the pep gene of A. fumigatus as potential PCR primers, which have not been tested
Isolation and characterization of mutants of Aspergillus niger deficient in extracellular proteases.
I E Mattern et al.
Molecular & general genetics : MGG, 234(2), 332-336 (1992-08-01)
In the present study, the extracellular protease activity in a strain of the filamentous fungus Aspergillus niger was investigated and mutant strains deficient in the production of extracellular proteases were isolated. The major protease, which is responsible for 80-85% of
D W Burdon
Journal of medical microbiology, 29(2), 145-157 (1989-06-01)
A novel replicating agent (IFDO) was isolated from ileal fluid. Growth occurred in vitro under aerobic and anaerobic conditions, and was faster at 37 degrees C than at room temperature. The doubling time was 15.8 min. Colonies were dark brown
S W Cho et al.
Acta crystallographica. Section D, Biological crystallography, 57(Pt 7), 948-956 (2001-06-22)
The crystal structure of aspergillopepsin I (AP) from Aspergillus phoenicis has been determined at 2.18 A resolution and refined to R and R(free) factors of 21.5 and 26.0%, respectively. AP has the typical two beta-barrel domain structure of aspartic proteinases.
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