Purification and biochemical properties of microbial pectinases—a review

TL;DR: Pectinases are one of the most widely distributed enzymes in bacteria, fungi and plants as discussed by the authors, and they have a share of 25% in the global sales of food enzymes.

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975 citations

Journal Article•DOI•

Plant protoplasts: status and biotechnological perspectives

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Michael R. Davey¹, Paul Anthony¹, J. Brian Power¹, Kenneth C. Lowe¹•Institutions (1)

University of Nottingham¹

01 Mar 2005-Biotechnology Advances

TL;DR: Novel approaches to maximise the efficiency of protoplast-to-plant systems include techniques already well established for animal and microbial cells, such as electrostimulation and exposure of protoplasts to surfactants and respiratory gas carriers, especially perfluorochemicals and hemoglobin.

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344 citations

Journal Article•DOI•

Pectin and Pectinases: Production, Characterization and Industrial Application of Microbial Pectinolytic Enzymes

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Danielle Biscaro Pedrolli, Alexandre Costa Monteiro, Eleni Gomes, Eleonora Cano Carmona¹•Institutions (1)

Sao Paulo State University¹

03 Mar 2009-The Open Biotechnology Journal

TL;DR: Departamento de Bioquimica e Microbiologia Instituto de Biociencias Universidade Estadual Paulista, UNESP, Avenida 24A, 1515, CEP 13506-900 Rio Claro, SP

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Abstract: Departamento de Bioquimica e Microbiologia Instituto de Biociencias Universidade Estadual Paulista, UNESP, Avenida 24A, 1515, CEP 13506-900 Rio Claro, SP

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284 citations

Cites background from "Purification and biochemical proper..."

...Properties of Some Purified Lyases Source Enzyme Optimum pH Optimum Temperature (°C) Reference Aspergillus japonicus PL 4.5-5.5 - [30] Aspergillus giganteus PL 8.5 50 [31] PGL (PeL I) 6.0 50 [18] PGL (PeL II) 4.6 50 [18] Aspergillus niger PGL (PeL III) 4.2 35 [18] Bacillus macerans PGL 8.0-8.5 63-67 [32] Bacillus pumilus PGL 8.5 70 [33] Bacillus sp. DT7 PL 8.0 60 [34] Bacillus sp. KSM-P7 PGL (Pel-7) 10.5 60-65 [35] Bacillus subtilis PGL (Pel C) 10.0 65 [36] PL 6.4 35 [37] Debaryomyces nepalensis PGL 7.5 32 [37] Grindamyl 3PA* PL 6.0 40 [38] Paenibacillus barcinonensis PGL (Pel A) 10.0 55 [36] Pectinase CCM* PL 6.0 40 [38] Pectinex 3XL* PL 5.0-6.5 35 [38] Penicillium canescens PL A 5.0-5.5 60 [28] Penicillium italicum PL (PNL) 6.0-7.0 50 [39] Rapidase C80* PL 6.0 40-45 [38] * Commercial names. lacturonase....
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...Acid pectinases, which are widely used in extraction, clarification, and removal of pectin in fruit juices, in maceration of vegetables to produce pastes and purées, and in winemaking, are often produced by fungi, especially Aspergillus niger ....
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...PGs are also important in some other fungi and bacteria virulence like Aspergillus flavus, Alternaria citri, Claviceps purpurea, Agrobacterium tumefaciens and Ralstonia solanacearum [51-53]....
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...Pectinases are abundantly produced by saprophytic fungi, and decaying plant tissue represents the most common substrate for pectinase-producing microorganisms [10]....
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...Van Alebeek and coworkers [29] conducted a detailed study of the action mode of pectin lyase A from Aspergillus niger which produces mono-, di-, tri- and tetragalacturonates, besides unsaturated di-, tri- and tetragalacturonates from methyloligogalacturonates....
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Book Chapter•DOI•

Microbial Enzymes of Use in Industry

[...]

Xiangyang Liu¹, Chandrakant Kokare•Institutions (1)

University of North Texas Health Science Center¹

01 Jan 2017

TL;DR: In this chapter, classification and microbial resources, microbial production, and industrial applications of a group of industrially used microbial enzymes, such as carbohydrases, proteases and lipases, are described.

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Abstract: A large variety of microorganisms produce potent biocatalysts as enzymes which vary in their microbial sources, chemical properties, and mechanisms. Usually, microbial enzymes catalyze the reactions of hydrolysis, oxidation, or reduction. Microbial enzymes have different active site motifs targeting diversified substrates. They may catalyze the reaction by completely different mechanisms even when they belong to the same class. Microbial enzymes are mainly produced by submerged fermentation and solid state fermentation. The enormous diversity of microbial enzymes makes them an interesting group of products for application in many areas such as agricultural, chemical industry, food processing industry, textile industry, pharmaceuticals, wood processing industry, analytical applications, cosmetics, and environmental pollution control, such as bioremediation and biodegradation. In this chapter, classification and microbial resources, microbial production, and industrial applications of a group of industrially used microbial enzymes, such as carbohydrases, proteases and lipases, are described.

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134 citations

Journal Article•DOI•

Microbial pectinase: sources, characterization and applications

[...]

Nevadita Sharma, Madhu Rathore, Mukesh Sharma

01 Mar 2013-Reviews in Environmental Science and Bio\/technology

TL;DR: This paper provides a bird’s eye view of the possible application of these enzymes in commercial sector and the molecular characterization of pectinolytic enzymes.

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Abstract: Today pectinases are upcoming industrially important bacterial enzymes. It can be produced by a variety of microorganisms. These enzymes act on pectin, which is the major component of middle lamella in plant cell wall. Pectinolytic enzymes are classified according to their mode of attack on the galacturonan part of the pectin molecules such as protopectinases, esterase’s and depolymerases. As we know that microbial enzymes work depends up on the type of enzymes application, temperature, concentration, and pH and so on, therefore, pectinase enzyme also differentiated according to their physical and chemical factors too. The biochemical structures of pectinases include members of all the major classes and the structure–function relationship, studies of a few available complexes of pectinases with substrate/analogs could be considered as prototypes for related family member and the molecular characterization of pectinolytic enzymes is also well documented. Furthermore, it provides a bird’s eye view of the possible application of these enzymes in commercial sector.

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127 citations

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Journal Article•DOI•

Applications of pectinases in the commercial sector: a review.

[...]

Des R. Kashyap¹, Pawan K. Vohra¹, Sidharth Chopra¹, Rupinder Tewari¹•Institutions (1)

Panjab University, Chandigarh¹

01 May 2001-Bioresource Technology

TL;DR: This review discusses various types of pectinases and their applications in the commercial sector.

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1,001 citations

Journal Article•DOI•

AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora

[...]

Yi-Hu Dong¹, Jin-Ling Xu, Xianzhen Li, Lian-Hui Zhang•Institutions (1)

National University of Singapore¹

28 Mar 2000-Proceedings of the National Academy of Sciences of the United States of America

TL;DR: The results indicate that the AI-inactivation approach represents a promising strategy for prevention of diseases in which virulence is regulated by AIs.

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Abstract: N-acylhomoserine lactones, known as autoinducers (AIs), are widely conserved signal molecules present in quorum-sensing systems of many Gram-negative bacteria. AIs are involved in the regulation of diverse biological functions, including expression of pathogenic genes in the plant pathogens Pseudomonas solanacearum, several Erwinia species, and the human pathogen Pseudomonas aeruginosa. A bacterial isolate, Bacillus sp. 240B1, is capable of enzymatic inactivation of AIs. The gene (aiiA) for AI inactivation from Bacillus sp. 240B1 has been cloned and shown to encode a protein of 250 amino acids. Sequence alignment indicates that AiiA contains a “HXHXDH” zinc-binding motif that is conserved in several groups of metallohydrolases. Site-directed mutagenesis showed that conserved aspartate and most histidine residues are required for AiiA activity. Expression of aiiA in transformed Erwinia carotovora strain SCG1 significantly reduces the release of AI, decreases extracellular pectolytic enzyme activities, and attenuates pathogenicity on potato, eggplant, Chinese cabbage, carrot, celery, cauliflower, and tobacco. Our results indicate that the AI-inactivation approach represents a promising strategy for prevention of diseases in which virulence is regulated by AIs.

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719 citations

Book Chapter•DOI•

Pectin, pectinase and protopectinase: production, properties, and applications

[...]

Takuo Sakai, Tatsuji Sakamoto, Johan Hallaert¹, Erick Vandamme¹•Institutions (1)

Ghent University¹

01 Jan 1993-Advances in Applied Microbiology

TL;DR: Research has been initiated with the aim of developing an improved alternative microbial pectin production process by means of a specific enzyme, called “protopectinase,” which solubilizes protopectin forming highly polymerized soluble pECTin.

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Abstract: Publisher Summary This chapter discusses the applications, properties, and production of pectin, pectinase, and protopectinase. Pectic substances are acid polysaccharides of high molecular weight that are widespread in the plant kingdom. The size, charge density, charge distribution, and degree of substitution of pectin molecules may be changed biologically or chemically. The pectins in these beverages are considered to be responsible for the “veloute” or “moeilleux” (softness or silkiness), which give the fruit product its particular character. The pectin production process consists mainly of an acid extraction, followed by a (partial) purification of the extract and, eventually, precipitation and drying. However, this process has several disadvantages that are addressed in the chapter. Research has been initiated with the aim of developing an improved alternative microbial pectin production process by means of a specific enzyme. The chapter also deals with a specific enzyme, called “protopectinase,” which solubilizes protopectin forming highly polymerized soluble pectin.

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395 citations

Journal Article•DOI•

Isolation of tobacco mesophyll cells in intact and active state

[...]

Itaru Takebe, Yoshiaki Otsuki, Shigeji Aoki

01 Jan 1968-Plant and Cell Physiology

275 citations

Journal Article•DOI•

Simultaneous saccharification and fermentation of lignocellulosic wastes to ethanol using a thermotolerant yeast.

[...]

S. Hari Krishna¹, T. Janardhan Reddy¹, G. V. Chowdary¹•Institutions (1)

Andhra University¹

01 Apr 2001-Bioresource Technology

TL;DR: Simultaneous saccharification and fermentation studies were carried out to produce ethanol from lignocellulosic wastes (sugar cane leaves and Antigonum leptopus leaves) using Trichoderma reesei cellulase and yeast cells and K. fragilis was found to perform better in the SSF process and result in high yields of ethanol.

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233 citations