Studies on the possible relationships of microbodies and multivesicular bodies to oxalate, endopolygalacturonase, and cellulase (Cx) production by Sclerotinia sclerotiorum

1972 ◽  
Vol 50 (8) ◽  
pp. 1743-1748 ◽  
Author(s):  
Douglas P. Maxwell ◽  
Paul H. Williams ◽  
Martha D. Maxwell
Keyword(s):  
Sclerotinia Sclerotiorum ◽  
Enzyme Production ◽  
Functional Role ◽  
Carbon Sources ◽  
Extracellular Enzyme ◽  
Ultrastructural Organization ◽  
Multivesicular Bodies ◽  
Membrane Bound ◽  
High Production

The possible functional role of vesicles and crystal-containing microbodies in the production of oxalate, endopolygalacturonase, or cellulase by Sclerotinia sclerotiorum was investigated. The presence of multivesicular bodies in hyphal tips was not correlated with secretion or production of oxalate or these extracellular hydrolases. More crystal-containing microbodies were present in hyphal tips grown on media which supported greater extracellular enzyme production. No correlation existed between numbers of crystal-containing microbodies in hyphal tips and production of oxalate. Numerous membrane-bound vesicles (0.09–0.18 µm diam) were associated with tips grown on a D-glucose–Na succinate medium which supported high production of oxalate. The general ultrastructural organization of these hyphal tips was similar to that reported for other ascomycetes. Differences in numbers and distributions of organelles were observed between hyphal tips and older hyphae as well as between hyphal tips grown on the different carbon sources.

The Role of Cross-Pathway Control Regulator CpcA in the Growth and Extracellular Enzyme Production of Penicillium oxalicum

2019 ◽  
Vol 77 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Yunjun Pan ◽  
Liwei Gao ◽  
Xiujun Zhang ◽  
Yuqi Qin ◽  
Guodong Liu ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Extracellular Enzyme ◽  
Penicillium Oxalicum

Regulation by amino acids of α-amylase and endo-β(1→4)-glucanase induction in mycelial culture of the mushroom Termitomyces clypeatus

1990 ◽  
Vol 36 (9) ◽  
pp. 617-624 ◽  
Author(s):  
Saswati Sengupta ◽  
S. Sengupta
Keyword(s):  
Amino Acids ◽  
Yeast Extract ◽  
Enzyme Production ◽  
Late Phase ◽  
Synthetic Medium ◽  
Extracellular Enzyme ◽  
Mycelial Culture ◽  
Termitomyces Clypeatus ◽  
Yeast Extract Medium

Termitomyces clypeatus constitutively liberated amyloglucosidase; the liberation was not repressed by glucose. Growth of the mushroom in synthetic medium was slow with starch, and only amyloglucosidase was liberated. Yeast extract stimulated growth and enzyme production in starch medium, and α-amylase along with amyloglucosidase was detected extracellularly. The mushroom could not utilise cellulose or liberate endo-β(1 → 4)-glucanase even when inducer cellobiose or glucose was added to cellulose at different concentrations. Cellobiose alone also failed to induce any extracellular endo-β(1 → 4)-glucanase production. Yeast extract in both cellulose and cellobiose media supported liberation of endo-β(1 → 4)-glucanase. Lactose was found to be a poor inducer even in yeast extract medium. However, both α-amylase and endo-β(1 → 4)-glucanase were detected intracellularly at a basal level even when the enzymes were absent extracellularly under inducing and noninducing conditions. The intracellular enzymes were only freely liberated into the medium in the presence of yeast extract. It appeared that induction of α-amylase and endo-β(1 → 4)-glucanase was largely inhibited by the restricted liberation of the enzymes in absence of yeast extract. Of the yeast extract components, amino acids were the active ingredient mimicking the role of yeast extract in induction. Yeast extract was found to relieve catabolic inhibition observed at the late phase of enzyme production. It is proposed that catabolic inhibition might have a role in the enzyme liberation and that amino acids supported extracellular enzyme production by relieving this inhibition. Key words: mushroom, Termitomyces clypeatus, catabolic inhibition, polysaccharidase induction, amino acid.

A membrane-bound plastid inclusion in the epidermis of leaves of Taraxacum officinale

1977 ◽  
Vol 55 (2) ◽  
pp. 222-225 ◽  
Author(s):  
E. S. Martin ◽  
G. Larbalestier
Keyword(s):  
Inclusion Bodies ◽  
Functional Role ◽  
Taraxacum Officinale ◽  
Single Membrane ◽  
Membrane Bound ◽  
Dense Inclusion ◽  
Electron Dense Inclusion

Epidermal chloroplasts of Taraxacum officinale agg. contain large electron-dense inclusion bodies enclosed by a single membrane. These inclusion bodies were not observed in mesophyll chloroplasts. The origin and functional role of these structures is discussed.

scholarly journals The Functional Role of Membrane Bound Proteinase 3

2010 ◽  
Vol 98 (3) ◽  
pp. 569a
Author(s):  
Torben Broemstrup ◽  
Nathalie Reuter
Keyword(s):  
Functional Role ◽  
Proteinase 3 ◽  
Membrane Bound

scholarly journals Extra- and intra-cellular lipases from a thermophilic Rhizopus oryzae and factors affecting their production

1993 ◽  
Vol 39 (10) ◽  
pp. 978-981 ◽  
Author(s):  
A. B. Salleh ◽  
R. Musani ◽  
M. Basri ◽  
K. Ampon ◽  
W. M. Z. Yunus ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Rhizopus Oryzae ◽  
Corn Steep Liquor ◽  
Carbon Sources ◽  
Extracellular Enzyme ◽  
Lipase Production ◽  
Intracellular Enzyme ◽  
Factors Affecting ◽  
Positive Effects ◽  
Steep Liquor

A thermophilic Rhizopus oryzae was isolated, and parameters affecting its production of extra- and intra-cellular lipases were investigated. All carbon sources tested with the exception of sucrose generally inhibited the production of extracellular lipase, but enhanced the production of intracellular lipase. Peptone was the best substrate for extracellular enzyme production, but for intracellular lipase production other substrates such as tryptone, tryptic soy digest, polypeptone, and corn steep liquor gave comparable results. Among lipid substrates, glycerol was the only stimulator of extracellular enzyme production, whereas olive oil, triolein, and oleic acid had very positive effects on intracellular enzyme production. Shaking enhanced the production of both types of enzymes; the temperature optima were 45 and 37 °C for extra- and intra-cellular lipases, respectively. A pH of 5.0 was optimal for production of both enzymes.Key words: lipases, Rhizopus oryzae, production.

scholarly journals Role of the PAS1 gene of Pichia pastoris in peroxisome biogenesis.

1994 ◽  
Vol 127 (5) ◽  
pp. 1259-1273 ◽  
Author(s):  
J A Heyman ◽  
E Monosov ◽  
S Subramani
Keyword(s):  
Pichia Pastoris ◽  
Biochemical Analysis ◽  
Sequence Similarity ◽  
Carbon Sources ◽  
Peroxisome Biogenesis ◽  
Daughter Cells ◽  
New Information ◽  
Membrane Bound ◽  
High Level

Several groups have reported the cloning and sequencing of genes involved in the biogenesis of yeast peroxisomes. Yeast strains bearing mutations in these genes are unable to grow on carbon sources whose metabolism requires peroxisomes, and these strains lack morphologically normal peroxisomes. We report the cloning of Pichia pastoris PAS1, the homologue (based on a high level of protein sequence similarity) of the Saccharomyces cerevisiae PAS1. We also describe the creation and characterization of P. pastoris pas1 strains. Electron microscopy on the P. pastoris pas1 cells revealed that they lack morphologically normal peroxisomes, and instead contain membrane-bound structures that appear to be small, mutant peroxisomes, or "peroxisome ghosts." These "ghosts" proliferated in response to induction on peroxisome-requiring carbon sources (oleic acid and methanol), and they were distributed to daughter cells. Biochemical analysis of cell lysates revealed that peroxisomal proteins are induced normally in pas1 cells. Peroxisome ghosts from pas1 cells were purified on sucrose gradients, and biochemical analysis showed that these ghosts, while lacking several peroxisomal proteins, did import varying amounts of several other peroxisomal proteins. The existence of detectable peroxisome ghosts in P. pastoris pas1 cells, and their ability to import some proteins, stands in contrast with the results reported by Erdmann et al. (1991) for the S. cerevisiae pas1 mutant, in which they were unable to detect peroxisome-like structures. We discuss the role of PAS1 in peroxisome biogenesis in light of the new information regarding peroxisome ghosts in pas1 cells.

The role of carbon sources in relation to pathogenicity of Sclerotinia sclerotiorum on Valencia peanut

2019 ◽  
Vol 99 (6) ◽  
pp. 824-833
Author(s):  
Phillip Lujan ◽  
Barry Dungan ◽  
Omar Holguin ◽  
Soum Sanogo ◽  
Naveen Puppala ◽  
...  
Keyword(s):  
Oxalic Acid ◽  
Sclerotinia Sclerotiorum ◽  
Acid Production ◽  
Agar Medium ◽  
Carbon Sources ◽  
Potato Dextrose Agar ◽  
Gas Chromatography Mass Spectrometry ◽  
Potato Dextrose Agar Medium ◽  
White Mycelium

Sclerotinia sclerotiorum is a necrotrophic fungal pathogen with a very wide host range. Isolates of this pathogen are normally described as having fluffy and white mycelium; however, isolates of S. sclerotiorum with darkly-pigmented mycelium on potato dextrose agar medium have been identified in eastern New Mexico and western Texas from Valencia peanut fields. Mutant non-pigmented S. sclerotiorum isolates (SW) were created in an earlier study from wild-type pigmented isolates (SD) using melanin inhibitors. The SD isolates were pathogenic on Valencia peanut, whereas the SW isolates were not. The current study was conducted to further characterize the differences between SD and SW isolates in regards to metabolite production and utilization, including the effects of carbon sources and oxalic acid precursors on oxalic acid production and pathogenicity on Valencia peanut. Gas chromatography–mass spectrometry (GC/MS) metabolomics analysis revealed a down-regulation of several sugars and compounds within the citric acid cycle as well as oxalic acid for SW isolates of S. sclerotiorum. The addition of glucose to potato dextrose agar medium allowed for the production of oxalic acid and restored pathogenicity in SW isolates that were previously non-pathogenic on Valencia peanut. This study indicates that glucose alone plays a major role in oxalic acid production and pathogenicity of S. sclerotiorum.

Screening of Alternative Carbon Sources for Recombinant Protein Production in Pichia pastoris

2016 ◽  
Vol 14 (1) ◽  
pp. 251-257 ◽  
Author(s):  
Gabriel Potvin ◽  
Zisheng Zhang ◽  
Amanda Defela ◽  
Howard Lam
Keyword(s):  
Pichia Pastoris ◽  
Enzyme Production ◽  
Recombinant Protein Production ◽  
Protein Production ◽  
Carbon Sources ◽  
Extracellular Enzyme ◽  
Fed Batch ◽  
Fermentation Time ◽  
Batch Cultures ◽  
Batch Bioreactor

AbstractSeventeen carbon sources were screened to identify those with the potential to support pGAP-regulated recombinant enzyme production by Pichia pastoris, using phytase as a model product. Of these, four, namely glucose, glycerol, fructose and ethanol, supported cell growth and enzyme production, and the performance of the latter two was analyzed. Ranges of acceptable residual carbon source concentrations, i.e. those at which no substrate-related growth inhibition occurred, were determined and used to design fed-batch bioreactor-based processes. In fed-batch cultures, fructose supported higher biomass concentrations and equivalent extracellular enzyme activities than glucose. The same metrics for the cultures grown on ethanol were comparable to those of the cultures grown on glucose, but with a greater required fermentation time.

scholarly journals MBTPS2, a membrane bound protease, underlying several distinct skin and bone disorders

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Natarin Caengprasath ◽  
Thanakorn Theerapanon ◽  
Thantrira Porntaveetus ◽  
Vorasuk Shotelersuk
Keyword(s):  
Functional Role ◽  
Cholesterol Homeostasis ◽  
Regulatory Proteins ◽  
Osteogenesis Imperfecta Type ◽  
Keratosis Follicularis ◽  
Cellular Processes ◽  
Unfolded Protein ◽  
Human Disorders ◽  
Membrane Bound

AbstractThe MBTPS2 gene on the X-chromosome encodes the membrane-bound transcription factor protease, site-2 (MBTPS2) or site-2 protease (S2P) which cleaves and activates several signaling and regulatory proteins from the membrane. The MBTPS2 is critical for a myriad of cellular processes, ranging from the regulation of cholesterol homeostasis to unfolded protein responses. While its functional role has become much clearer in the recent years, how mutations in the MBTPS2 gene lead to several human disorders with different phenotypes including Ichthyosis Follicularis, Atrichia and Photophobia syndrome (IFAP) with or without BRESHECK syndrome, Keratosis Follicularis Spinulosa Decalvans (KFSD), Olmsted syndrome, and Osteogenesis Imperfecta type XIX remains obscure. This review presents the biological role of MBTPS2 in development, summarizes its mutations and implicated disorders, and discusses outstanding unanswered questions.

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