Article

Detergent proteases.

Henkel, Enzyme Technology, Henkelstrasse 67 40191, Duesseldorf, Germany.
Current Opinion in Biotechnology (Impact Factor: 8.04). 09/2004; 15(4):330-4. DOI: 10.1016/j.copbio.2004.06.005
Source: PubMed

ABSTRACT Over the past 20 years, the development of subtilisins as typical detergent proteases has employed all the tools of enzyme technology, resulting in a constant flow of new and improved enzymes. The number of molecules identified and characterized, however, is in clear opposition to the number of molecules that are entering the market. Will the next-generation detergent proteases be based on new backbones different from subtilisins, or will the use of all available technologies (rational design, directed evolution and exploitation of natural diversity) yield improved subtilisins, ending the current era dominated by high alkaline subtilisins? These questions will have to be answered not only by the performance of the molecules themselves, but also by their yield in fermentation and their compatibility with existing production technologies.

1 Bookmark
 · 
332 Views
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: In the presented paper, the influence of the molecular weight and the type of polyamino acid functional groups on the electrokinetic properties and the stability of chromium (III) oxide suspension were examined. Analysis of the data obtained from the adsorption, potentiometric titration, zeta potential, and stability measurements allows to propose stabilization or destabilization mechanism of the studied systems. In the studies, there were used polyamino acids with different ionic characters: anionic polyaspartic acid and cationic polylysine. The measurements showed that the zeta potential depends on the concentration and molecular weight of the applied polymer. Stability of the chromium (III) oxide suspensions in the presence of ionic polyamino acids increases compared to the results obtained in the absence of polymers. The exception is LYS 4,900 at pH = 10. Under these conditions, the decrease in stability is observed due to formation of polymer bridges between the polymer chains adsorbed on different colloidal particles. Determination of the stabilization/destabilization mechanism of the polyamino acid/chromium (III) oxide system and examination of the effects of polymer molecular weight on the stabilization properties can contribute to a wider use of this group of compounds as potential stabilizers or flocculants in many industrial suspensions.
    Colloid and Polymer Science 10/2014; 292(10):2453-2464. · 2.16 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Bacillus clausii I-52 which produced SDS- and -tolerant extracellular alkaline protease (BCAP) was isolated from heavily polluted tidal mud flat of West Sea in Incheon, Korea and stable strain (transformant C5) of B. clausii I-52 harboring another copy of BCAP gene in the chromosome was developed using the chromosome integration vector, pHPS9-fuBCAP. When investigated the production of BCAP using B. clausii transformant C5 through pilot-scale submerged fermentation (500 L) at for 30 h with an aeration rate of 1 vvm and agitation rate of 250 rpm, protease yield of approximately 105,700 U/mL was achieved using an optimized medium (soybean meal 2%, wheat flour 1%, sodium citrate 0.5%, 0.4%, 0.1%, NaCl 0.4%, 0.01%, 0.05%, liquid maltose 2.5%, 0.6%). The enzyme stability of BCAP was increased by addition of polyols (10%, v/v) and also, the stabilities of BCAP towards not only the thermal-induced inactivation at but also the SDS and -induced inactivation at were enhanced. Among the polyols examined, the best result was obtained with propylene glycol (10%, v/v). The BCAP supplemented with propylene glycol exhibited extreme stability against not only the detergent components such as -orephin sulfonate (AOS) and zeolite but also the commercial detergent preparations. The granulized enzyme of BCAP was prepared with approximately 1,310,000 U/g of granule. Wash performance analysis using EMPA test fabrics revealed that BCAP granule exhibited high efficiency for removal of protein stains in the presence of anionic surfactants as well as bleaching agents. When compared to Savinase 6T and Everlase 6T manufactured by Novozymes, BCAP under this study probably showed similar or higher efficiency for the removal of protein stains. These results suggest that the alkaline protease produced from B. clausii transformant C5 showing high stability against detergents and high wash performance has significant potential and a promising candidate for use as a detergent additive.
    KSBB Journal. 01/2012; 27(6).
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Since volatile and rising cost factors such as energy, raw materials and market competitiveness have a significant impact on the economic efficiency of biotechnological bulk productions, industrial processes need to be steadily improved and optimized. Thereby the current production hosts can undergo various limitations. To overcome those limitations and in addition increase the diversity of available production hosts for future applications, we suggest a Production Strain Blueprinting (PSB) strategy to develop new production systems in a reduced time lapse in contrast to a development from scratch.To demonstrate this approach, Bacillus pumilus has been developed as an alternative expression platform for the production of alkaline enzymes in reference to the established industrial production host Bacillus licheniformis. To develop the selected B. pumilus as an alternative production host the suggested PSB strategy was applied proceeding in the following steps (dedicated product titers are scaled to the protease titer of Henkel's industrial production strain B. licheniformis at lab scale): Introduction of a protease production plasmid, adaptation of a protease production process (44%), process optimization (92%) and expression optimization (114%). To further evaluate the production capability of the developed B. pumilus platform, the target protease was substituted by an alpha-amylase. The expression performance was tested under the previously optimized protease process conditions and under subsequently adapted process conditions resulting in a maximum product titer of 65% in reference to B. licheniformis protease titer. In this contribution the applied PSB strategy performed very well for the development of B. pumilus as an alternative production strain. Thereby the engineered B. pumilus expression platform even exceeded the protease titer of the industrial production host B. licheniformis by 14%. This result exhibits a remarkable potential of B. pumilus to be the basis for a next generation production host, since the strain has still a large potential for further genetic engineering. The final amylase titer of 65% in reference to B. licheniformis protease titer suggests that the developed B. pumilus expression platform is also suitable for an efficient production of non-proteolytic enzymes reaching a final titer of several grams per liter without complex process modifications.
    Microbial Cell Factories 03/2014; 13(1):46. · 3.31 Impact Factor

Full-text (2 Sources)

Download
588 Downloads
Available from
May 21, 2014