Crystalline Bacterial Proteinase

Hagihara, Bunji; Nakai, M.; Matsubara, Hiroshi; Komaki, Toshiaki; Yonetani, Takashi; Okunuki, Kazuo

doi:10.1093/oxfordjournals.jbchem.a126856

Cited by 210 publications

(39 citation statements)

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“…Assay of proteinase and protein measurement. The proteolytic activity was measured by a modification of the Kunitz casein digestion method, 9 > which was used as the standard method in this study. Samples of 1.0 ml of an enzyme solution were mixed with 5.0 ml of a substrate solution containing 0.6% (wfv) casein in 0.1 M Naphosphate buffer (pH 7.6).…”

Section: Methodsmentioning

confidence: 99%

Isolation and Characterization of a Possible Native Cucumisin from Developing Melon Fruits and Its Limited Autolysis to Cucumisin

Yamagata

Ueno

Iwasaki

1989

Agricultural and Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Isolation and Characterization of a Possible Native Cucumisin from Developing Melon Fruits and Its Limited Autolysis to Cucumisin

Yamagata

Ueno

Iwasaki

1989

Agricultural and Biological Chemistry

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“…Protease activity was determined as described by Hagihara et al (1958), 1ml of suitably diluted enzyme was mixed with 1ml of casein Yadav et al 8631 (1% w/v prepared in 50 mM carbonate-bicarbonate buffer of pH 10.0). The mixture was incubated at 37 °C for 10 min.…”

Section: Enzyme Assaymentioning

confidence: 99%

Oxidant and solvent stable alkaline protease from Aspergillus flavus and its characterization

Santosh¹,

Bisht²,

Shikha³

et al. 2011

Afr. J. Biotechnol.

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The increase in agricultural practices has necessitated the judicious use of agricultural wastes into value added products. In this study, an extracellular, organic solvent and oxidant stable, serine protease was produced by Aspergillus flavus MTCC 9952 under solid state fermentation. Maximum protease yield was obtained when the strain was grown under wheat bran and corn cob mixture (1:1) incubated for 48 h at pH 9.0 and temperature 37°C with 50% of initial moisture content. The partially purified enzyme showed wide range of pH optima (8.0-12.0) and pH stability (7.0-12.0), whereas, optimum temperature was 40°C and was stable over a wide range of temperature 30-45°C. The protease was extremely stable towards several organic solvents. The enzyme retained 80% of its original activity in the presence of non ionic and ionic surfactants and 100% with 10% H 2 O 2 after 1 h of incubation at 30°C. In addition, the enzyme showed excellent compatibility with some commercial powder detergents. The compatibility of our protease with several detergents, oxidants and organic solvents suggests its possible use in detergent industry and peptide synthesis.

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“…The agglutination test was judged positive when the erythrocytes were not suspended back into the supernatant solution by gentle shaking. The trypsin inhibitory activity was determined by using casein as substrate (16 of 2% acrinol solution precipitated some contaminants and left the lethal protein in solution. A typical elution pattern of the CM-cellulose chromatography is shown in Fig.…”

Section: Discussionmentioning

confidence: 99%

The isolation and characterization of a lethal protein from kintoki beans (Phaseolus vulgaris).

Hamaguchi

Yagi

Nishino

et al. 1977

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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Crystalline Bacterial Proteinase

Cited by 210 publications

References 0 publications

Isolation and Characterization of a Possible Native Cucumisin from Developing Melon Fruits and Its Limited Autolysis to Cucumisin

Isolation and Characterization of a Possible Native Cucumisin from Developing Melon Fruits and Its Limited Autolysis to Cucumisin

Oxidant and solvent stable alkaline protease from Aspergillus flavus and its characterization

The isolation and characterization of a lethal protein from kintoki beans (Phaseolus vulgaris).

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