• Title/Summary/Keyword: bleach-stable

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Production of Bleach-Stable and Halo-Tolerant Alkaline Protease by an Alkalophilic Bacillus pumilus JB05 Isolated from Cement Industry Effluents

  • Johnvesly, B.;Naik, Gajanan R.
    • Journal of Microbiology and Biotechnology
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    • v.11 no.4
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    • pp.558-563
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    • 2001
  • A new alkalophilic strain of Bacillus pumilus JB¬05 producing bleach-stable and halo-tolerant alkaline protease was isolated from cement industry effluents in Karnataka, India. The effects of carbon and nitrogen sources on protease production by this alkalophilic strain were observed after a 30-h incubation. A high level of alkaline protease activity was obtained in the presence of starch as the carbon and peptone as the nitrogen sources. The partially purified enzyme showed an optimum temperature and pH activity at $58^{\circ}C$ and 10.5, respectively. The enzyme was completely inhibited by PMSF (95.0%) indicating it as a serine protease. It is bleach-stable as it retained 35% original activity in the presence of 10% (v/v) hydrogen peroxide at $30^{\circ}$C after 2 h and is halo-tolerant as it retained 70% original activity in the presence of 2.5 M sodium chloride at $30^{\circ}C$ after 2 h incubation.

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Conservation of the Old Hat

  • Im Sung-Kyung;Han Myung-Sook
    • The International Journal of Costume Culture
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    • v.7 no.2
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    • pp.151-157
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    • 2004
  • This research is to conservate the old hat and restore its shape and place it on a supportive form in a stable protective container. The hat is a homemade construction, utilizing three different machine made laces, and two cotton net fabrics. The exterior, particularly the top crown piece, as well as the lace along the brim's edge has been generally soiled and discolored. Inside the crown, the cotton net has broken threads, and thread loss in several areas. The paper covering the two wires is very weak, and has discolored the lace in the areas of contact. The plastic buckles of the velvet ribbon have also discolored the areas where there is contact. The wash/bleach bath procedure was very effective. Virtually all of the light brown surface discoloration stains were removed. The darker brown spots, particularly concentrated around the two paper covered wires and assumed to be rust, were $90\%$ removed by the treatment. The brown spots apparently were due to the degradation of the paper covering, and not caused by the wire itself. The buckram foundation lost about $50\%$ of its stiffness, but this was not a major concern due to the fact that this hat should remain it its mount, which has been designed to serve for both storage and exhibition purposes.

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Biochemical Characterization of a Novel Alkaline and Detergent Stable Protease from Aeromonas veronii OB3

  • Manni, Laila;Misbah, Asmae;Zouine, Nouhaila;Ananou, Samir
    • Microbiology and Biotechnology Letters
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    • v.48 no.3
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    • pp.358-365
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    • 2020
  • An organic solvent- and bleach-stable protease-producing strain was isolated from a polluted river water sample and identified as Aeromonas veronii OB3 on the basis of biochemical properties (API 20E) and 16S rRNA sequence analysis. The strain was found to hyper-produce alkaline protease when cultivated on fish waste powder-based medium (HVSP, 4080 U/ml). The biochemical properties and compatibility of OB3 with several detergents and additives were studied. Maximum activity was observed at pH 9.0 and 60℃. The crude protease displayed outstanding stability to the investigated surfactants and oxidants, such as Tween 80, Triton X-100, and H2O2, and almost 36% residual activity when incubated with 1% SDS. Remarkably, the enzyme demonstrated considerable compatibility with commercial detergents, retaining more than 100% of its activity with Ariel and Tide (1 h, 40℃). Moreover, washing performance of Tide significantly improved by the supplementation of small amounts of OB3 crude protease. These properties suggest the potential use of this alkaline protease as a bio-additive in the detergent industry and other biotechnological processes such as peptide synthesis.