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Journal ArticleDOI

Purification and characterization of an alkaline pectin lyase from Aspergillus flavus

01 May 2008-Process Biochemistry (Elsevier)-Vol. 43, Iss: 5, pp 547-552
TL;DR: An alkaline pectin lyase secreted by Aspergillus flavus MTCC 7589 was purified to electrophoretic homogeneity using ammonium sulphate fractionation, anion exchange chromatography on DEAE cellulose and gel filtration chromatography in order to show efficacy in retting of Crotalaria juncea fibers.
About: This article is published in Process Biochemistry.The article was published on 2008-05-01. It has received 67 citations till now. The article focuses on the topics: Pectin lyase & Ammonium.
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Journal ArticleDOI
TL;DR: Departamento de Bioquimica e Microbiologia Instituto de Biociencias Universidade Estadual Paulista, UNESP, Avenida 24A, 1515, CEP 13506-900 Rio Claro, SP
Abstract: Departamento de Bioquimica e Microbiologia Instituto de Biociencias Universidade Estadual Paulista, UNESP, Avenida 24A, 1515, CEP 13506-900 Rio Claro, SP

284 citations

Journal ArticleDOI
TL;DR: This review tries to fill the gap by providing all relevant information exclusively for pectin lyase by covering structural aspects, substrate specificity, molecular biology, biotechnological applications and future prospects of pECTin lyases.

215 citations

Journal ArticleDOI
TL;DR: This paper reviews the scientific information available on pECTin structure, pectin-modifying enzymes, and the use of enzymes to produce pect in with controlled structure or pectIn-derived oligosaccharides, with functional or nutritional interesting properties.
Abstract: Pectins are complex branched polysaccharides present in primary cell walls. As a distinctive feature, they contain high amount of partly methyl-esterified galacturonic acid and low amount of rhamnose and carry arabinose and galactose as major neutral sugars. Due to their structural complexity, they are modifiable by many different enzymes, including hydrolases, lyases, and esterases. Their peculiar structure is the origin of their physicochemical properties. Among others, their remarkable gelling properties make them a key additive for food industries. Pectin-degrading enzymes and -modifying enzymes may be used in a wide variety of applications to modulate pectin properties or produce pectin derivatives and oligosaccharides with functional as well as nutritional interests. This paper reviews the scientific information available on pectin structure, pectin-modifying enzymes, and the use of enzymes to produce pectin with controlled structure or pectin-derived oligosaccharides, with functional or nutritional interesting properties.

100 citations

Journal ArticleDOI
TL;DR: The scanning electron microscopic analysis confirmed that alkali followed by enzymatic treatment effectively removed non-cellulosic gummy material from the fiber; hence, this enzyme mixture may find feasible applications in the fiber and textile industry.
Abstract: The present study demonstrated the simultaneous production and optimization of pectinolytic enzymes (pectate lyase and polygalacturonase) under SSF from Bacillus tequilensis SV11-UV37 using wheat bran as a substrate, which is commercially viable and cost-effective. Optimization by one variable-at-a-time-approach showed a maximum yield of pectate lyase (1371.25 U/gds) and polygalacturonase (85.45 U/gds) with wheat bran using 80 % (v/w) moisture, 0.7 mm particle size, 20 % (v/w) inoculum, 1 % (w/w) pectin at 37 °C, pH 6 and 72 h of incubation. In addition, optimization using central composite design achieved 1.6-fold improvement in both pectate lyase (1828.13 U/gds) and polygalacturonase (105.55 U/gds) yield at optimum levels of pectin (3 %, w/w), inoculum size (20 %, v/w) and moisture level (80 %, v/w). Further, Retting studies concluded that the enzyme mixture was efficient in separating the whole fiber from kenaf and part (>75 %) from sunn hemp. In degumming of sunn hemp fibers, amount of galacturonic acid released and percentage weight loss was higher in successive alkali and enzymatic treatment than their independent treatments. The scanning electron microscopic analysis also confirmed that alkali followed by enzymatic treatment effectively removed non-cellulosic gummy material from the fiber; hence, this enzyme mixture may find feasible applications in the fiber and textile industry.

50 citations

Journal ArticleDOI
TL;DR: The thermostable and alkaline nature of this pectinase can meet the demand of various industrial processes like paper and pulp industry, in textile industry, fruit juice industry, plant tissue maceration and wastewater treatment.
Abstract: Pectinase enzymes are one of the commercially important enzymes having great potential in various industries especially in food industry. Pectinases accounts for 25 % of global food enzymes produced and their market is increasing day by day. Therefore, the exploration of microorganism with novel characteristics has always been the focus of the research. Microorganism dwelling in unique habitat may possess unique characteristics. As such, a pectinase producing fungus Aspergillus niger strain MCAS2 was isolated from soil of Manaslu Conservation Area (MCA), Gorkha, Nepal. The optimum production of pectinase enzyme was observed at 48 h of fermentation. The pectinase enzyme was partially purified by cold acetone treatment followed by Sephadex G-75 gel filtration chromatography. The partially purified enzyme exhibited maximum activity 60 U/mg which was almost 8.5-fold higher than the crude pectinase. The approximate molecular weight of the enzyme was found to be 66 kDa as observed from SDS-PAGE. The pectinase enzyme was active at broad range of temperature (30–70 °C) and pH (6.2–9.2). Optimum temperature and pH of the pectinase enzyme were 50 °C and 8.2 respectively. The enzyme was stable up to 70 °C and about 82 % of pectinase activity was still observed at 100 °C. The thermostable and alkaline nature of this pectinase can meet the demand of various industrial processes like paper and pulp industry, in textile industry, fruit juice industry, plant tissue maceration and wastewater treatment. In addition, the effect of different metal ions on pectinase activity was also studied.

50 citations

References
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Journal Article
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.

289,852 citations


"Purification and characterization o..." refers methods in this paper

  • ...Protein was determined by the Lowry method [12] taking Bovine serum albumin as the standard....

    [...]

Journal ArticleDOI
15 Aug 1970-Nature
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Abstract: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

232,912 citations


Additional excerpts

  • ...3 kDa) as standard proteins [13,14]....

    [...]

Journal Article
01 Jan 1970-Nature
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Abstract: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products. Four major components of the head are cleaved during the process of assembly, apparently after the precursor proteins have assembled into some large intermediate structure.

203,017 citations

Journal ArticleDOI
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.

19,381 citations

Book
01 Nov 1991
TL;DR: In this article, basic laboratory techniques for isolation, cultivation, and cultural characterisation of microorganisms are described, including basic techniques for isolating, culturing, and characterizing microorganisms.
Abstract: I: Basic Laboratory Techniques for Isolation, Cultivation, and Cultural Characterization of Microorganisms. II: Microscopy. III: Bacterial Staining. IV: Cultivation of Microorganisms: Nutritional and Physical Requirements, and Enumeration of Microbial Populations. V: Biochemical Activities of Microorganisms. VI: The Protozoa. VII: The Fungi. VIII: The Viruses. IX: Physical and Chemical Agents for the Control of Microbial Growth. X: Microbiology of Food. XI: Microbiology of Water. XII: Microbiology of Soil. XIII: Bacterial Genetics. XIV: Medical Microbiology. XV: Immunology. Appendices.

1,931 citations