Industrially Important Carbohydrate Degrading Enzymes from Yeasts: Pectinases, Chitinases, and β-1,3-Glucanases
01 Jan 2009-pp 673-691
About: The article was published on 2009-01-01. It has received 2 citations till now. The article focuses on the topics: Chitinase & Pectinase.
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TL;DR: This review is an account of experiences of two research teams (from Italy to Spain); the leading idea is the following: yeasts represent valuable sources in food science and microbiology and are a kind of food factories, because of the potentiality of whole cells or for their produced compounds.
Abstract: This review is an account of experiences of two research teams (from Italy to Spain); the leading idea is the following: yeasts represent valuable sources in food science and microbiology and are a kind of food factories, because of the potentiality of whole cells or for their produced compounds. This review covers three major areas: the first section addresses the role of yeasts as starter cultures with a special focus on wine. The second section is an update on probiotic yeasts. Finally, the focus of the last section is on enzymes produced by yeasts, with a short description of the removal of mycotoxin.
46 citations
Cites background from "Industrially Important Carbohydrate..."
...These pectic substances need to be removed in order to remove turbidity and prevent cloud-forming spoilage (Gummadi et al. 2009)....
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01 Jan 2014
TL;DR: In this paper, an investigation to find Pectinase enzyme with low cost production using Penicillium lividum and Aspergillus sp strain in liquid state fermentation was conducted.
Abstract: In this work an investigation to find Pectinase enzyme with low cost production. These studies deal with to produce Pectinase enzyme using Penicillium sp strain in liquid state fermentation. Agro-industrial residues used as carbon sources were orange peel, mosambi peel, pineapple, wheat bran, papaya and pectin.Best pectinolytic activity, as indicated by the diameter of clear, hydrolyzed zones on the medium plates containing commercial citrus pectin as sole carbon source, was obtained with Penicillium lividum using pineapple closely followed by Aspergillus sps using orange peel.The optimum temperature was found to be 30˚C and pH at 8.0. Peak pectinase activity of 397mg/ml and 346mg/ml protein was respectively obtained by Liquid State Fermentation (LSF) at 48 h for Penicillium lividum and Aspergillus sps. The strains of Penicillium lividum and Aspergillus sps have good prospect for Pectinase production. Pineapple peel and orange peel is a good low-cost fermentation substrate for pectinase production by the investigated fungus.
1 citations
References
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TL;DR: The view of critical questions regarding pectin structure, biosynthesis, and function that need to be addressed in the coming decade are presented and new methods that may be useful to study localized pectins in the plant cell wall are described.
1,795 citations
TL;DR: This review of recent advances in understanding chitin synthesis and its degradation in insects will summarize recent advances.
Abstract: Chitin is one of the most important biopolymers in nature. It is mainly produced by fungi, arthropods and nematodes. In insects, it functions as scaffold material, supporting the cuticles of the epidermis and trachea as well as the peritrophic matrices lining the gut epithelium. Insect growth and morphogenesis are strictly dependent on the capability to remodel chitin-containing structures. For this purpose, insects repeatedly produce chitin synthases and chitinolytic enzymes in different tissues. Coordination of chitin synthesis and its degradation requires strict control of the participating enzymes during development. In this review, we will summarize recent advances in understanding chitin synthesis and its degradation in insects.
1,037 citations
TL;DR: It is reported here that the main proteinaceous inhibitor of fungal growth in bean leaves is chitinase, an enzyme that can be induced by the plant hormone ethylene, or by pathogen attack.
Abstract: The antimicrobial arsenal of plants is thought to consist mainly of secondary metabolites, among which the phytoalexins are the best-studied1–3. But plants may also possess antimicrobial proteins4,5: it has been reported that wheat-germ agglutinin, a chitin-binding lectin from wheat embryos, inhibits growth of the fungus Trichoderma viride4. This has led to the notion that plant lectins, with their intriguing biochemical similarity to animal antibodies, have an antibody-like antimicrobial function4,6,7. We report here that the main proteinaceous inhibitor of fungal growth in bean leaves is chitinase, an enzyme that can be induced by the plant hormone ethylene, or by pathogen attack. Among commercial preparations of purified chitin-binding lectins (from wheat germ, tomato, potato, pokeweed and gorse), only those containing contaminating chitinase activity inhibit fungal growth. Our data indicate that plant chitinases, but not chitin-binding lectins, are important antifungal proteins in plants.
915 citations
TL;DR: The phylogenetic diversity of an oligotrophic marine picoplankton community was examined by analyzing the sequences of cloned ribosomal genes, and sequences obtained from two phylogenetic groups of organisms that are not closely related to any known rRNA sequences from cultivated organisms.
Abstract: The phylogenetic diversity of an oligotrophic marine picoplankton community was examined by analyzing the sequences of cloned ribosomal genes. This strategy does not rely on cultivation of the resident microorganisms. Bulk genomic DNA was isolated from picoplankton collected in the north central Pacific Ocean by tangential flow filtration. The mixed-population DNA was fragmented, size fractionated, and cloned into bacteriophage lambda. Thirty-eight clones containing 16S rRNA genes were identified in a screen of 3.2 x 10(4) recombinant phage, and portions of the rRNA gene were amplified by polymerase chain reaction and sequenced. The resulting sequences were used to establish the identities of the picoplankton by comparison with an established data base of rRNA sequences. Fifteen unique eubacterial sequences were obtained, including four from cyanobacteria and eleven from proteobacteria. A single eucaryote related to dinoflagellates was identified; no archaebacterial sequences were detected. The cyanobacterial sequences are all closely related to sequences from cultivated marine Synechococcus strains and with cyanobacterial sequences obtained from the Atlantic Ocean (Sargasso Sea). Several sequences were related to common marine isolates of the gamma subdivision of proteobacteria. In addition to sequences closely related to those of described bacteria, sequences were obtained from two phylogenetic groups of organisms that are not closely related to any known rRNA sequences from cultivated organisms. Both of these novel phylogenetic clusters are proteobacteria, one group within the alpha subdivision and the other distinct from known proteobacterial subdivisions. The rRNA sequences of the alpha-related group are nearly identical to those of some Sargasso Sea picoplankton, suggesting a global distribution of these organisms. Images
872 citations
01 Jan 1990
TL;DR: This edition of Microbial Enzymes and Biotechnol ogy has attempted to bring together accounts (by the relevant experts) of the current status of the major areas of enzyme technology and specifically those areas of actual and/or potential commercial importance.
Abstract: Biotechnology is now one of the major growth areas in science and engineering and within this broad discipline enzyme technology is one of the areas earmarked for special and significant developments. This publication is the second edition of Microbial Enzymes and Biotechnol ogy which was originally published in 1983. In this edition the editors have attempted to bring together accounts (by the relevant experts) of the current status of the major areas of enzyme technology and specifically those areas of actual and/or potential commercial importance. Although the use of microbial enzymes may not have expanded at quite the rate expected a decade ago, there is nevertheless intense activity and considerable interest in the whole area of enzyme technology. Microbial enzymes have been used in industry for many centuries although it is only comparatively recently that detailed knowledge relating to their nature, properties and function has become more evident. Developments in the 1960s gave a major thrust to the use of microbial enzymes in industry. The commercial success of alkaline proteases and amyloglucosidases formed a bed-rock for subsequent research and development in the area."
518 citations