Article

Detergent proteases.

Henkel, Enzyme Technology, Henkelstrasse 67 40191, Duesseldorf, Germany.
Current Opinion in Biotechnology (Impact Factor: 7.86). 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
 · 
305 Views
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Detergent enzymes account for about 30% of the total worldwide production of enzymes and are one of the largest and most successful applications of modern industrial biotechnology. Proteases can improve the wash performance of household, industrial, and institutional laundry detergents used to remove protein-based stains such as blood, grass, body fluids, and food soils. This article describes two easy and cheap laboratory exercises to study the presence, profile, and basic enzymology of detergent proteases. These laboratory practicals are based on the determination of the detergent protease activity of various commercial detergents using the N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine p-nitroanilide method and the bovine serum albumin degradation capacity. Students are also required to elucidate the enzymatic subtype of detergent proteases by studying the inhibitory potential of several types of protease inhibitors revealed by the same experimental methodology. Additionally, the results of the exercises can be used to provide additional insights on elementary enzymology by studying the influence of several important parameters on protease activity such as temperature (in this article) and the influence of pH and effects of surfactants and oxidizers (proposed). Students also develop laboratory skills, problem-solving capacities, and the ability to write a laboratory report. The exercises are mainly designed for an advanced undergraduate project in the biochemistry and biotechnology sciences. Globally, these laboratory practicals show students the biotechnological applications of proteases in the detergent industry and also reinforce important enzymology concepts.
    Biochemistry and Molecular Biology Education 07/2011; 39(4):280-90. · 0.70 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The psychrophilic protease subtilisin S41 from the Antarctic bacillus TA41, and two variants with two and seven amino acid substitutions were studied using molecular dynamics simulation at 283 and 363 K. The analysis of protein dynamics revealed that the average global flexibility of both variants was slightly higher than wild type at both 283 and 363 K. Essential dynamics analysis evidenced that the most relevant collective motions, especially at 363 K, differ in distribution and intensity for each protein variant. At high temperature and for the thermo labile wild type, an amplification of a subset of the low-temperature largest collective motions was observed. On the other hand, the two thermostable variants showed a rather different pattern of essential motions at 363 K from those at 283 K. These results support the hypothesis that the introduced amino acid substitutions, rather than improving the global stability of the variants by increasing its rigidity, lead to a change on the principal fluxional modes allowing the protein to explore a different subset of conformations. A better understanding of this process can open alternative strategies to increase the enzyme stability in addition to increasing the rigidity of the protein scaffold.
    Protein Engineering Design and Selection 04/2011; 24(7):533-44. · 2.59 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Many real-life stains have origins from biological matters including proteins, lipids and carbohydrates that act as gluing agents binding along with other particulates or microbes to exposed surfaces of automobiles, furniture and fabrics. Mimicking naturally occurring self-defensive processes, we demonstrate in this work that a solid surface carrying partially exposed enzyme granules protected the surface in situ from contamination by biological stains and fingerprints. Attributed to the activities of enzymes which can be made compatible with a wide range of materials, such anti-contamination and self-cleaning functionalities are highly selective and efficient toward sticky chemicals. This observation promises a new mechanism in developing smart materials with desired anti-microbial, self-reporting, self-cleaning or self-healing functions. Biotechnol. Bioeng. © 2013 Wiley Periodicals, Inc.
    Biotechnology and Bioengineering 01/2013; · 4.16 Impact Factor

Full-text (2 Sources)

View
525 Downloads
Available from
May 21, 2014