Characteristics of mutants designed to incorporate a new ion pair into the structure of a cold adapted subtilisin-like serine proteinase

Sigurðardóttir, Anna Guðný; Arnórsdóttir, Jóhanna; Thorbjarnardóttir, Sigrídur H.; Eggertsson, Guðmundur; Suhre, Karsten; Kristjánsson, Magnús M.

doi:10.1016/j.bbapap.2008.11.018

Cited by 22 publications

(14 citation statements)

References 43 publications

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“…Mutations at these sites will be interesting to test, in order to better disclose structure-function relationship in the different temperature-adapted subtilisins. In this context, it has been previously reported, that an extra saltbridge (15-257) in VPR has effect on kinetic parameters (Sigurdardóttir et al, 2009), pointing out the relevance of electrostatic interactions in influencing cold-adapted enzyme properties. Moreover, the D138-R169 ionic pair could have a relevant role in the protein dynamics.…”

Section: Discussionmentioning

confidence: 96%

“…The investigation of the differences in electrostatic interactions with a dynamic approach among extremophilic homologs allows to enrich the current view on electrostatic interactions and temperature adaptation (Elcock, 1998;Nussinov, 2002, 2004;Papaleo et al, 2007;Sigurdardóttir et al, 2009;Thomas and Elcock, 2004), highlighting one more time their crucial role. In fact, thermophiles are generally characterized by an increased number of surface charges and ionic networks with a dominant role in enhancing thermostability.…”

Section: Discussionmentioning

confidence: 98%

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Dynamic properties of extremophilic subtilisin-like serine-proteases

Tiberti

Papaleo

2011

Journal of Structural Biology

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 98%

Dynamic properties of extremophilic subtilisin-like serine-proteases

Tiberti

Papaleo

2011

Journal of Structural Biology

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“…The thermostability and activity of subtilisin-like serine proteinase [VPR] had been improved by SDM approach [146]. Such studies clearly indicate that it is possible to improve one character [activity/stability] without affecting the other.…”

Section: Enhancing Thermo-stability Of Cold-active Proteasesmentioning

confidence: 99%

Biotechnology of Cold-Active Proteases

Joshi

Satyanarayana

2013

Biology

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The bulk of Earth’s biosphere is cold (<5 °C) and inhabited by psychrophiles. Biocatalysts from psychrophilic organisms (psychrozymes) have attracted attention because of their application in the ongoing efforts to decrease energy consumption. Proteinases as a class represent the largest category of industrial enzymes. There has been an emphasis on employing cold-active proteases in detergents because this allows laundry operations at ambient temperatures. Proteases have been used in environmental bioremediation, food industry and molecular biology. In view of the present limited understanding and availability of cold-active proteases with diverse characteristics, it is essential to explore Earth’s surface more in search of an ideal cold-active protease. The understanding of molecular and mechanistic details of these proteases will open up new avenues to tailor proteases with the desired properties. A detailed account of the developments in the production and applications of cold-active proteases is presented in this review.

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“…In order to compensate for the lower washing efficiency at decreased temperatures, enzyme producers have devoted much R&D capacity to screen for new proteolytic enzymes which are more suitable for washing at lower temperatures. Recently there has been growing interest in psychrophilic/psychrotolerant enzymes as models in basic studies to investigate the thermal stability of proteins and to understand the relationship between their stability, flexibility, catalytic efficiency, and as potential candidates for R&D and biotechnological applications (Gerday et al 2000;Siguroardottir et al 2009). …”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a cold active alkaline protease from Stenotrophomonas sp., isolated from Kashmir, India

Saba

Qazi

Rather

et al. 2011

World J Microbiol Biotechnol

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A Psychrotolerant alkaline protease producing bacterium IIIM-ST045 was isolated from a soil sample collected from the Thajiwas glacier of Kashmir, India and identified as Stenotrophomonas sp. on the basis of its biochemical properties and 16S ribosomal gene sequencing. The strain could grow well within a temperature range of 4-37°C however, showed optimum growth at 15°C. The strain was found to over-produce proteases when it was grown in media containing lactose as carbon source (157.50 U mg(-1)). The maximum specific enzyme activity (398 U mg(-1)) was obtained using soya oil as nitrogen source, however, the inorganic nitrogen sources urea, ammonium chloride and ammonium sulphate showed the lowest production of 38.9, 62.2 and 57.9 U mg(-1). The enzyme was purified to 18.45 folds and the molecular weight of the partially purified protease was estimated to be ~55 kDa by SDS-PAGE analysis. The protease activity increased as the increase in enzyme concentration while as the optimum enzyme activity was found when casein (1% w/v) was used as substrate. The enzyme was highly active over a wide range of pH from 6.5 to 12.0 showing optimum activity at pH 10.0. The optimum temperature for the enzyme was 15°C. Proteolytic activity reduced gradually with higher temperatures with a decrease of 56% at 40°C. The purified enzyme was checked for the removal of protein containing tea stains using a silk cloth within a temperature range of 10-60°C. The best washing efficiency results obtained at low temperatures indicate that the enzyme may be used for cold washing purposes of delicate fabrics that otherwise are vulnerable to high temperatures.

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Characteristics of mutants designed to incorporate a new ion pair into the structure of a cold adapted subtilisin-like serine proteinase

Cited by 22 publications

References 43 publications

Dynamic properties of extremophilic subtilisin-like serine-proteases

Dynamic properties of extremophilic subtilisin-like serine-proteases

Biotechnology of Cold-Active Proteases

Purification and characterization of a cold active alkaline protease from Stenotrophomonas sp., isolated from Kashmir, India

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