Characterization of detergent stable and feather degrading serine proteases from Bacillus mojavensis A21

Haddar, Anissa; Kamoun, Amel; Fakhfakh-Zouari, Nahed; Hmidet, Noomen; Nasri, Monçef

doi:10.1016/j.bej.2010.05.002

Cited by 49 publications

(27 citation statements)

References 58 publications

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“…Interestingly, MP1 alkaline protease was more stable than the commercial detergent protease Purafect ® 2000E, towards all the solid detergents tested under the same conditions. Incubated at 50 • C with Axion, the MP1 protease retains more than 90% of its initial activity, whereas Purafect ® 2000E retains less than 60% of its initial activity [36]. The high stability of MP1 alkaline protease is a very important indicator of enzyme compatibility with laundry detergents.…”

Section: Effects Of Surfactants Oxidizing Agents and Laundry Detergementioning

confidence: 99%

Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a detergent additive and for shrimp waste deproteinization

Jellouli

Ghorbel-Bellaaj

Ayed

et al. 2011

Process Biochemistry

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111

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Section: Effects Of Surfactants Oxidizing Agents and Laundry Detergementioning

confidence: 99%

Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a detergent additive and for shrimp waste deproteinization

Jellouli

Ghorbel-Bellaaj

Ayed

et al. 2011

Process Biochemistry

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111

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“…SDS can unfold most proteins through the interactions between its charged head group and the positively charged amino acid side chains of proteins, as well as through the interactions between the alkyl chain of SDS and the non-polar regions on the surface and in the interior of proteins [14]. Stability in the presence of SDS is considered to be an important factor in industrial enzymes because few SDS-stable enzymes have been reported thus far [15]. In contrast to SDS, Triton X-100 had no effect on the activity of detergent enzymes.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the activity and stability of amylase from saliva and detergent: Laboratory practicals for studying the activity and stability of amylase from saliva and various commercial detergents

Valls

Rojas

Pujadas

et al. 2012

Biochem Molecular Bio Educ

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This article presents two integrated laboratory exercises intended to show students the role of α‐amylases (AAMYs) in saliva and detergents. These laboratory practicals are based on the determination of the enzymatic activity of amylase from saliva and different detergents using the Phadebas test (quantitative) and the Lugol test (qualitative) under different conditions (e.g. variations in temperature and alkalinity). This work also proposes the study of enzyme stability in the presence of several surfactants and oxidizing agents using the same technical approach. The proposed laboratory exercises promote the understanding of the physiological function of this enzyme and the biotechnological applications of AAMYs in the detergent industry. The exercises also promote the understanding that the enzymatic stability and performance are dependent on the organism of origin, and if necessary, these properties could be modified by genetic engineering. In addition, this article reinforces the development of laboratory skills, problem‐solving capabilities, and the ability to write a laboratory report. The exercises are proposed primarily as an undergraduate project for advanced students in the biochemical and biotechnological sciences. These laboratory practicals are complementary to the previously published BAMBED article (Biochemistry and Molecular Biology Education Vol. 39, No. 4, pp. 280–290, 2011) on detergent proteases.

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“…Use of the crude and partially purified enzymes is preferred over purified preparation to avoid the cost of purification and make the processes commercially viable. Recently, the applications of surfactant and detergent compatible crude protease from Bacillusmojavensis have been studied (Anissa et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Hide Dehairing and Laundry Detergent Compatibility Testing of Thermostable and Solvents Tolerant Alkaline Protease from Hot Spring Isolate <i>Bacillus cohnii</i>U3

Dudhgara¹,

Sunil²,

Ghelani³

2015

OnLine Journal of Biological Sciences

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Abstract:In the present study, alkaline protease producing thermophilic Bacillus cohniiU3 strain was isolation from Unnai hot spring, India. The maximum production of protease (344 U/mL) was reported after 72 h of inoculation at 50°C in shake flask culture using the gelatin casein medium. The protease was found to remain active up to 96 h and production was growth dependent. The activity of parital purified protease was reported in abroad range of pH ranging from 4.0 to 11.0 with an optimum of 9.0 pH; Enzymes was indicated the highest activity at 50°C temperature. Salt independent catalysis and activity with a broad range of substrate concentration is the key feature of the protease. Thermos table nature, the stability in alkaline pH and stability in high salt concentration for 45 min were outstanding features of protease. The enzyme was stable in the presence of various organic solvents like Dimethyl Sulphoxide (DMSO), Methanol, Butanol, n-Hexane, Benzene at 25% (v/v) concentration. A good compatibility of the enzyme with most commercial detergents indicated its application in detergent industry. The remarkable dehairing in goat hide and destaining of blood spot in 2 h using 10 U/mL of protease assure that it could be a potential candidate for leather and detergent industries.

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Characterization of detergent stable and feather degrading serine proteases from Bacillus mojavensis A21

Cited by 49 publications

References 58 publications

Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a detergent additive and for shrimp waste deproteinization

Alkaline-protease from Bacillus licheniformis MP1: Purification, characterization and potential application as a detergent additive and for shrimp waste deproteinization

Characterization of the activity and stability of amylase from saliva and detergent: Laboratory practicals for studying the activity and stability of amylase from saliva and various commercial detergents

Hide Dehairing and Laundry Detergent Compatibility Testing of Thermostable and Solvents Tolerant Alkaline Protease from Hot Spring Isolate <i>Bacillus cohnii</i>U3

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