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Mukesh Kapoor

Bio: Mukesh Kapoor is an academic researcher from Central Food Technological Research Institute. The author has contributed to research in topics: Xylanase & Pectinase. The author has an hindex of 23, co-authored 42 publications receiving 3124 citations. Previous affiliations of Mukesh Kapoor include Council of Scientific and Industrial Research & University of Delhi.
Topics: Xylanase, Pectinase, Chemistry, Medicine, Fermentation

Papers
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TL;DR: This review will focus on complex xylan structure and the microbial enzyme complex involved in its complete breakdown, studies on xylanase regulation and production and their potential industrial applications, with special reference to biobleaching.
Abstract: Despite an increased knowledge of microbial xylanolytic systems in the past few years, further studies are required to achieve a complete understanding of the mechanism of xylan degradation by microorganisms and their enzymes. The enzyme system used by microbes for the metabolism of xylan is the most important tool for investigating the use of the second most abundant polysaccharide (xylan) in nature. Recent studies on microbial xylanolytic systems have generally focussed on induction of enzyme production under different conditions, purification, characterization, molecular cloning and expression, and use of enzyme predominantly for pulp bleaching. Rationale approaches to achieve these goals require a detailed knowledge of the regulatory mechanism governing enzyme production. This review will focus on complex xylan structure and the microbial enzyme complex involved in its complete breakdown, studies on xylanase regulation and production and their potential industrial applications, with special reference to biobleaching.

1,339 citations

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TL;DR: A thermostable and cellulase-free xylanase has been produced from Streptomyces sp.

208 citations

Journal ArticleDOI
TL;DR: Xylanase and pectinase were stable over a broad pH range between 5.4 and 9.0, respectively, retaining more than 85% of their activity, and were optimally active at 60°C.
Abstract: Streptomyces sp. QG-11-3, which produces a cellulase-free thermostable xylanase (96 IU ml−1) and a pectinase (46 IU ml−1), was isolated on Horikoshi medium supplemented with 1% w/v wheat bran. Carbon sources that favored xylanase production were rice bran (82 IU ml−1) and birch-wood xylan (81 IU ml−1); pectinase production was also stimulated by pectin and cotton seed cake (34 IU ml−1 each). The partially purified xylanase and pectinase were optimally active at 60°C. Both enzymes were 100% stable at 50°C for more than 24 h. The half-lives of xylanase and pectinase at 70, 75 and 80°C were 90, 75 and 9 min, and 90, 53 and 7 min, respectively. The optimum pH values for xylanase and pectinase were 8.6 and 3.0, respectively, at 60°C. Xylanase and pectinase were stable over a broad pH range between 5.4 and 9.4 and 2.0 to 9.0, respectively, retaining more than 85% of their activity. Ca2+ stimulated the activity of both enzymes up to 7%, whereas Cd2+, Co2+, Cr3+, iodoacetic acid and iodoacetamide inhibited xylanase up to 35% and pectinase up to 63%; at 1 mM, Hg2+ inhibited both enzymes completely. Journal of Industrial Microbiology & Biotechnology (2000) 24, 396–402.

171 citations

Journal ArticleDOI
TL;DR: In this article, an alkaline (optimum pH 10.0) and thermo stable polygalacturonase from Bacillus sp. MG-cp-2 has been applied for the degumming of Ramie ( Boehmeria nivea ) and sunn hemp ( Crotalaria juncea ) bast fibres.

157 citations

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TL;DR: It is proposed that the purified enzyme from S. cyaneus SN32 is an endoxylanase and belongs to Group 1 xylanases (low molecular weight - basic proteins), and easy purification from the fermentation broth and its high stability will be highly useful for industrial application of this end oxylanase.

144 citations


Cited by
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Journal ArticleDOI
TL;DR: An up-to-date review of the literature available on the subject of liquid bio-fuels can be found in this article, which includes information based on the research conducted globally by scientists according to their local socio-cultural and economic situations.

1,948 citations

Journal ArticleDOI
TL;DR: The adaptation strategies of the extremophilic xylanases isolated to date and the potential industrial applications of these enzymes will also be presented.
Abstract: Xylanases are hydrolytic enzymes which randomly cleave the β 1,4 backbone of the complex plant cell wall polysaccharide xylan. Diverse forms of these enzymes exist, displaying varying folds, mechanisms of action, substrate specificities, hydrolytic activities (yields, rates and products) and physicochemical characteristics. Research has mainly focused on only two of the xylanase containing glycoside hydrolase families, namely families 10 and 11, yet enzymes with xylanase activity belonging to families 5, 7, 8 and 43 have also been identified and studied, albeit to a lesser extent. Driven by industrial demands for enzymes that can operate under process conditions, a number of extremophilic xylanases have been isolated, in particular those from thermophiles, alkaliphiles and acidiphiles, while little attention has been paid to cold-adapted xylanases. Here, the diverse physicochemical and functional characteristics, as well as the folds and mechanisms of action of all six xylanase containing families will be discussed. The adaptation strategies of the extremophilic xylanases isolated to date and the potential industrial applications of these enzymes will also be presented.

1,584 citations

Journal ArticleDOI
TL;DR: The types and sources of proteases, protease yield-improvement methods, the use of new methods for developing novel proteases and applications of alkaline proteases in industrial sectors are discussed, with an overview on the use in the detergent industry.
Abstract: Proteolytic enzymes are ubiquitous in occurrence, being found in all living organisms, and are essential for cell growth and differentiation. The extracellular proteases are of commercial value and find multiple applications in various industrial sectors. Although there are many microbial sources available for producing proteases, only a few are recognized as commercial producers. A good number of bacterial alkaline proteases are commercially available, such as subtilisin Carlsberg, subtilisin BPN′ and Savinase, with their major application as detergent enzymes. However, mutations have led to newer protease preparations with improved catalytic efficiency and better stability towards temperature, oxidizing agents and changing wash conditions. Many newer preparations, such as Durazym, Maxapem and Purafect, have been produced, using techniques of site-directed mutagenesis and/or random mutagenesis. Directed evolution has also paved the way to a great variety of subtilisin variants with better specificities and stability. Molecular imprinting through conditional lyophilization is coming up to match molecular approaches in protein engineering. There are many possibilities for modifying biocatalysts through molecular approaches. However, the search for microbial sources of novel alkaline proteases in natural diversity through the "metagenome" approach is targeting a hitherto undiscovered wealth of molecular diversity. This fascinating development will allow the biotechnological exploitation of uncultured microorganisms, which by far outnumber the species accessible by cultivation, regardless of the habitat. In this review, we discuss the types and sources of proteases, protease yield-improvement methods, the use of new methods for developing novel proteases and applications of alkaline proteases in industrial sectors, with an overview on the use of alkaline proteases in the detergent industry.

1,573 citations

Journal ArticleDOI
TL;DR: In this article, a comprehensive state of the art describing the advancement in recent pretreaments, metabolic engineering approaches with special emphasis on the latest developments in consolidated biomass processing, current global scenario of bioethanol pilot plants and biorefinery concept for the production of biofuels and bioproducts.

1,369 citations

Journal ArticleDOI
TL;DR: The various hemicelluloses structures present in lignocellulose, the range of pre-treatment and hydrolysis options including the enzymatic ones, and the role of different microbial strains on process integration aiming to reach a meaningful consolidated bioprocessing are reviewed.

1,355 citations