Application of cellulases from an alkalothermophilic <i>Thermomonospora</i> sp. in biopolishing of denims

Anish, Ramakrishnan; Rahman, Mohammad Safikur; Rao, Mala

doi:10.1002/bit.21175

Cited by 94 publications

(53 citation statements)

References 15 publications

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“…The biotechnological potential of cellulases is currently being exploited in industrial processes, e.g., in the paper, textile, and detergent industries (6,35,57). However, the paucity of enzymes that efficiently hydrolyze cellulose under the harsh conditions required by the specific processes represents a serious limit in the development of industrial-scale biomass breakdown (26).…”

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confidence: 99%

Cellulose Degradation by Sulfolobus solfataricus Requires a Cell-Anchored Endo-β-1-4-Glucanase

2012

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A sequence encoding a putative extracellular endoglucanase (sso1354) was identified in the complete genome sequence of Sulfolobus solfataricus. The encoded protein shares signature motifs with members of glycoside hydrolases family 12. After an unsuccessful first attempt at cloning the full-length coding sequences in Escherichia coli, an active but unstable recombinant enzyme lacking a 27-residue N-terminal sequence was generated. This 27-amino-acid sequence shows significant similarity with corresponding regions in the sugar binding proteins AraS, GlcS, and TreS of S. solfataricus that are responsible for anchoring them to the plasma membrane. A strategy based on an effective vector/host genetic system for Sulfolobus and on expression control by the promoter of the S. solfataricus gene which encodes the glucose binding protein allowed production of the enzyme in sufficient quantities for study. In fact, the enzyme expressed in S. solfataricus was stable and highly thermoresistant and showed optimal activity at low pH and high temperature. The protein was detected mainly in the plasma membrane fraction, confirming the structural similarity to the sugar binding proteins. The results of the protein expression in the two different hosts showed that the SSO1354 enzyme is endowed with an endo-␤-1-4-glucanase activity and specifically hydrolyzes cellulose. Moreover, it also shows significant but distinguishable specificity toward several other sugar polymers, such as lichenan, xylan, debranched arabinan, pachyman, and curdlan.

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Cellulose Degradation by Sulfolobus solfataricus Requires a Cell-Anchored Endo-β-1-4-Glucanase

2012

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“…The biostoning of denim generally involves the use of acid and neutral cellulases, which have the undesirable property of causing back staining of indigo dye. Alkaline or alkali-stable cellulases, which can diminish indigo back staining under higher pH, are recommended for further improvement of the process 38 .…”

Section: Cellulasesmentioning

confidence: 99%

Industrial Important Enzymes from Alkaliphiles – An overview

Chinnathambi¹

2015

Biosci., Biotech. Res. Asia

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Alkaliphiles are an interesting group of extremophilic organisms that thrive at pH of 9.0 and above and which are represented by prokaryotes, eukaryotes, and archaea. It is clear that a variety of taxa are represented among the alkaliphiles, some of which are new. Alkaliphiles can be isolated from normal environments such as garden soil, although the number isolated increases dramatically in highly alkaline environments. Many alkaliphile products, notably enzymes, have found widespread practical applications, primarily in the detergent and laundry industries; other potentially important products isolated from alkaliphiles include antibiotics and carotenoids. Alkaliphiles, and their products, are also potentially important for use in the degradation of xenobiotics, and they play a major role in the biogeocycling of key inorganic compounds. This review provides an insight into the huge diversity of alkaliphilic bacteria, the varied products obtained from them, and the need for further investigations on this interesting group of bacteria.

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“…Cellulase treatment of denim fabric is an environment-friendly method compared to with stone washing. 12,13 Otherwise, cellulases are utilized to improve the appearance of cellulosic garments by removing fuzz fibers and pills from the surface. Because the amorphous region of cellulose causes fuzz and pill formation on the garment surface, using a single type cellulase, preferentially endoglucanase, will be sufficient for removing fuzz and pill of amorphous cellulose.…”

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confidence: 99%

“…Because the amorphous region of cellulose causes fuzz and pill formation on the garment surface, using a single type cellulase, preferentially endoglucanase, will be sufficient for removing fuzz and pill of amorphous cellulose. 13 The purpose of this study was to determine some properties (optimum pH, temperature, thermal stability, and kinetic properties) of EG from a local isolate Trichoderma atroviride. Otherwise, the paper presents the effect of EG on the properties of pretreated lignocellulosic wastes and denim fabric.…”

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Industrial Applications of Endoglucanase Obtained from Novel and Native Trichoderma atroviride

Şahin

Özmen

Bıyık

2016

Chem.Biochem.Eng.Q.

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An endo-β-1,4-glucanase (EG), produced under submerged fermentation by local isolate Trichoderma atroviride, was purified using ammonium sulfate precipitation, column and ion exchange chromatography with 55.16 fold and a specific activity of 30.9 EU mg -1 . The studies of PAGE, SDS-PAGE and zymogram test have been carried out. The EG had optimum activity at pH 5.0 and 50 °C respectively. Using CMC as substrate, the enzyme showed maximum activity (V max ) of 6.7 (µmol glucose min . While the EG activity was activated by NaCl, inhibited by MgCl 2 and MgSO 4 . Otherwise, Tween 80, Triton X-100 and the total saponins known as biosurfactants enhanced the EG activity. The obtained EG had low K m and high thermal stability. Additionally, usability of the EG in biotechnological application was investigated. The results showed that the EG had potentially sufficient effects on denim fabric and pretreated lignocellulosic wastes.

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Application of cellulases from an alkalothermophilic Thermomonospora sp. in biopolishing of denims

Cited by 94 publications

References 15 publications

Cellulose Degradation by Sulfolobus solfataricus Requires a Cell-Anchored Endo-β-1-4-Glucanase

Cellulose Degradation by Sulfolobus solfataricus Requires a Cell-Anchored Endo-β-1-4-Glucanase

Industrial Important Enzymes from Alkaliphiles – An overview

Industrial Applications of Endoglucanase Obtained from Novel and Native Trichoderma atroviride

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