Production of pectolytic and macerating enzyme by Phoma strasseri

1972 ◽  
Vol 18 (7) ◽  
pp. 1065-1072 ◽  
Author(s):  
Hassan A. Melouk ◽  
Chester E. Horner
Keyword(s):  
Enzyme Activity ◽  
Phenolic Compounds ◽  
Enzyme Activities ◽  
Viscosity Reduction ◽  
Pectic Substances ◽  
Pectolytic Enzymes ◽  
Reduction Assay ◽  
Pectolytic Enzyme

Pectolytic enzyme activity of P. strasseri was highest in filtrates from cultures 5 and 23 days old, as determined by reducing-groups assay (RGA). Pectolytic enzyme activity, as determined by viscosity-reduction assay (VRA), was highest in cultures 7 days old. Macerating enzyme activities were highest in cultures 10 days old. Young peppermint-rhizome sections were more susceptible to maceration by P. strasseri filtrates than older sections. Colored phenolic compounds were released from macerated rhizomes and amounts released were correlated with degree of maceration.Differential inhibition of pectolytic enzyme activity (as judged by VRA and RGA assays) by a range of phenolic compounds suggests that at least two pectolytic enzymes capable of hydrolyzing α-1,4 linkages of pectic substances are produced by P. strasseri.Highest activities of pectolytic and macerating enzyme in extracts from diseased rhizomes were detected 5 days after inoculation with P. strasseri. Extracts from healthy rhizomes did not show pectolytic and macerating enzyme activity.Healthy peppermint-rhizome tissues had higher activities of polyphenoloxidase than diseased tissues; also, polyphenoloxidase activities in inoculated rhizomes decreased as time of incubation increased.

Effect of relative humidity on production of extracellular pectolytic enzymes by Botrytis cinerea and Sclerotinia sclerotiorum

1969 ◽  
Vol 47 (6) ◽  
pp. 1007-1010 ◽  
Author(s):  
L. Van Den Berg ◽  
S. M. Yang
Keyword(s):  
Enzyme Activity ◽  
Relative Humidity ◽  
Botrytis Cinerea ◽  
Sclerotinia Sclerotiorum ◽  
Nutrient Solution ◽  
Nutrient Medium ◽  
Enzyme Production ◽  
Pectic Substances ◽  
Pectolytic Enzymes ◽  
Pectolytic Enzyme

B. cinerea and S. sclerotiorum growing in a nutrient medium on the surface of carrots at 20 °C produced significantly more extracellular pectolytic enzymes when the carrots were exposed to 94–96% relative humidity than when exposed to 98–100% relative humidity. Tests in which these organisms were grown in a nutrient solution containing pectic substances showed that they produced pectolytic enzymes in significant quantities only when readily metabolizable sources of energy (e.g. ethanol, carbohydrates) were not available. These results suggest that the low relative humidity increased enzyme production by concentrating nutrients on the carrot surface to the point where they inhibited growth of the organisms and stimulated enzyme production. Tests also showed that pectolytic enzyme activity on the surface of unwashed carrots stored 9 months at 0–1 °C was substantially higher at 90–95% relative humidity than at 98–100% relative humidity. The results indicated that reduced decay at 98–100% relative humidity was largely due to lower pectolytic enzyme production.

Variations and correlations within and between morphology, pathogenicity, and pectolytic enzyme activity in Sclerotinia from Saskatchewan

1972 ◽  
Vol 50 (4) ◽  
pp. 767-786 ◽  
Author(s):  
R. A. A. Morrall ◽  
L. J. Duczek ◽  
J. W. Sheard
Keyword(s):  
Host Species ◽  
Enzyme Activities ◽  
Pectin Methylesterase ◽  
Defined Medium ◽  
Discrete Groups ◽  
Pectolytic Enzymes ◽  
Pathogenicity Tests ◽  
Pectolytic Enzyme

One hundred and fourteen isolates of Sclerotinia from 23 different hosts in many parts of Saskatchewan were grouped, according to their morphology, on minimal medium. Two types of seedling pathogenicity tests on six host species were conducted on at least one isolate from each morphological group and one from each host species. A total of 38 isolates was tested. Assays for pectolytic enzyme activities of the same 38 isolates were done using a defined medium, and Swede turnip and carrot tissue as substrates. Polygalacturonase, pectin transeliminase, and pectin methylesterase were all tested. The results showed that an endopolygalacturonase was probably the most prevalent enzyme. Some isolates also produced exopolygalacturonase and pectin methylesterase, but pectin transeliminase was never detected. There was no correlation between pathogenicity of the isolates and their enzyme activities in vitro or in vivo, suggesting that pectolytic enzymes are not responsible alone for pathogenicity. Agglomerative classification was used to demonstrate relationships between the isolates. However, the isolates did not fall into discrete groups based on morphological, pathological, physiological, or even combined characteristics. Neither were there clear host or geographic associations. This continuous variation rather than a segregated population is consistent with Purdy's "broader concept of the species S. sclerotiorum."

scholarly journals Rat uterine microbiochemistry: metabolic enzyme activities stimulated by 17-beta-estradiol are localized in epithelial cells.

1987 ◽  
Vol 35 (6) ◽  
pp. 657-662 ◽  
Author(s):  
J P Holt ◽  
E Rhe
Keyword(s):  
Enzyme Activity ◽  
Smooth Muscle ◽  
Epithelial Cells ◽  
Dose Response ◽  
Enzyme Activities ◽  
Time Course ◽  
Citrate Synthase ◽  
Ovariectomized Rats ◽  
Similar Response ◽  
Estradiol Treatment

Lactate dehydrogenase (LDH; EC 1.1.1.27), citrate synthase (CS; EC 4.1.3.7), and beta-hydroxyacyl-CoA-dehydrogenase (beta-OH-acyl-CoA-DH; EC 1.1.1.35) activities were determined in each of the three major cell types of rat uterus, i.e., epithelial, stromal, and smooth muscle, using quantitative microanalytical techniques. Adult ovariectomized rats were treated with 17-beta-estradiol to determine the time course and dose response (0.025-50 micrograms/300-g rat) effect of estrogen on enzyme activity of each type of uterine cell. The use of "oil well" and enzyme-cycling microtechniques to determine the time course and the dose responses of enzyme activity changes required microassays involving 1595 microdissected single cell specimens. Estradiol treatment increased epithelial LDH, CS and beta-OH-acyl-CoA-DH activity but had no effect on these enzymes in the stroma or in smooth muscle cells. The estradiol-stimulated peak enzyme activities on Day 4 in the intervention group are compared with those in the ovariectomized rat controls as follows: LDH, 44.5 +/- 3.5 vs 22.3 +/- 3.9; CS, 3.5 +/- 0.2 vs 1.5 +/- 0.6; beta-OH-acyl-CoA-H, 3.5 +/- 0.32 vs 2.2 +/- 0.2 (mean +/- standard deviation; mol/kg/hr). Stromal cell activities (LDH, 7.4 +/- 1.0; CS, 1.2 +/- 0.2; beta-OH-acyl-CoA-DH, 0.9 +/- 0.1) were significantly lower than epithelial cell levels and were similar to smooth muscle levels. Therefore, even in the ovariectomized animal epithelial cells have markedly higher metabolic activity compared with adjacent cells. The enzyme activities are expressed as moles of substrate reacting per kilogram of dry weight per hour. All three enzymes exhibited a 17-beta-estradiol-induced dose response between 0.025-0.15 micrograms/300-g rat. The three enzymes studied all had similar response patterns to estrogen. The effect of estradiol was restricted to epithelial cells, with enzyme activities increasing to maximal levels after approximately 96 hr of hormone treatment. This study therefore not only confirms the specific and differential metabolic responses of uterine cells to estradiol treatment, but clearly demonstrates that marked metabolic differences exist between epithelial cells and stromal or smooth muscle uterine cells.

Change Analysis of Enzyme Activity under Different Conditions of Film Remnant in Soil

2012 ◽  
Vol 518-523 ◽  
pp. 39-43
Author(s):  
Xiao Guang Zhao ◽  
Yuan Yuan Guan ◽  
Wen Yu Huang
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Scientific Basis ◽  
Soil Enzyme ◽  
Soil Microorganism ◽  
Soil Enzyme Activities ◽  
Change Analysis ◽  
Soil Material ◽  
The Relationship

In this paper, simulated experiments were performed in pots by using soil materials in different conditions of film remnant. Based on the research on soil microorganism quantity trends of soil enzyme activities were analyzed systematically: soil without film remnant, soil with film remnant for 5, 10, 15 and 20 years. By analyzing crop progress, the relationship with soil material was studied, in order to provide scientific basis for the variation laws between different conditions of film remnant and the activity of soil enzyme.

scholarly journals Interaction of soluble glucosyl- and mannosyl-transferase enzyme activities in the synthesis of a glucomannan

1972 ◽  
Vol 129 (3) ◽  
pp. 645-655 ◽  
Author(s):  
J. S. Heller ◽  
C. L. Villemez
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Enzyme Preparation ◽  
The Other ◽  
Acceptor Molecule ◽  
Soluble Enzyme ◽  
Phaseolus Aureus ◽  
Polymeric Product ◽  
Sugar Nucleotide ◽  
Solubilized Enzyme

A neutral-detergent-solubilized-enzyme preparation derived from Phaseolus aureus hypocotyls contains two types of glycosyltransferase activity. One, mannosyltransferase enzyme activity, utilizes GDP-α-d-mannose as the sugar nucleotide substrate. The other, glucosyltransferase enzyme activity, utilizes GDP-α-d-glucose as the sugar nucleotide substrate. The soluble enzyme preparation catalyses the formation of what appears to be a homopolysaccharide when either sugar nucleotide is the only substrate present. A β-(1→4)-linked mannan is the only polymeric product when only GDP-α-d-mannose is added. A β-(1→4)-linked glucan is the only polymeric product when only GDP-α-d-glucose is added. In the presence of both sugar nucleotides, however, a β-(1→4)-linked glucomannan is formed. There are indications that endogenous sugar donors may be present in the enzyme preparation. There appear to be only two glycosyltransferases in the enzyme preparation, each catalysing the transfer of a different sugar to the same type of acceptor molecule. The glucosyltransferase requires the continual production of mannose-containing acceptor molecules for maintenance of enzyme activity, and is thereby dependent upon the activity of the mannosyltransferase. The mannosyltransferase, on the other hand, does not require the continual production of glucose-containing acceptors for maintenance of enzyme activity, but is severely inhibited by GDP-α-P-glucose. These properties promote the synthesis of β-(1→4)-linked glucomannan rather than β-(1→4)-linked glucan plus β-(1→4)-linked mannan when both sugar nucleotide substrates are present.

scholarly journals Research Progress of Sirtuin4 in Cancer

2021 ◽  
Vol 10 ◽  
Author(s):  
Yibing Bai ◽  
Jiani Yang ◽  
Ying Cui ◽  
Yuanfei Yao ◽  
Feng Wu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Enzyme Activity ◽  
Energy Metabolism ◽  
Nicotinamide Adenine Dinucleotide ◽  
Enzyme Activities ◽  
Research Progress ◽  
Diverse Range ◽  
Catalytic Activities ◽  
Cellular Processes ◽  
Dependent Protein

Sirtuins (SIRTs) are members of the silent information regulator-2 family. They are a conserved family of nicotinamide adenine dinucleotide-dependent protein lysine deacylases. SIRTS are involved in intricate cellular processes. There are seven subtypes of SIRTs (1–7) in mammals. SIRT4 is located mainly in mitochondria and has various catalytic activities. These enzyme activities give it a diverse range of important biologic functions, such as energy metabolism, oxidative stress, and aging. Cancer is characterized as reprogramming of energy metabolism and redox imbalance, and SIRT4 can affect tumorigenesis. Here, we review the structure, localization, and enzyme activity of SIRT4 and its role in various neoplasms.

scholarly journals Proteolytische Aktivitäten der lysosomalen Enzyme bei Milchrindern* – 3. Mitteilung: Beziehungen der Energie- und Eiweißversorgung zur lysosomalen Enzymaktivität im Blutplasma beim Milchrind

2000 ◽  
Vol 43 (1) ◽  
pp. 17-26
Author(s):  
L. Panicke ◽  
J. Weingärtner ◽  
M. Schmidt ◽  
T. Król
Keyword(s):  
Enzyme Activity ◽  
Food Intake ◽  
Dairy Cows ◽  
Milk Production ◽  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
Correlation Coefficients ◽  
Food Ration ◽  
Milk Performance ◽  
Relationship Of

Abstract. Title of the paper: Relationship between lysosomal blood activity and milk content» of urea and protein in different phases of milk production in dairy cows Relationship of lysosomal enzyme activities in blood and supply of energy and protein in dairy cattle were investigated. Closed correlation coefficients were calculated for lysosomal enzyme activity and content of protein and urea in milk. Especially a high or a low content of protein in the food ration affects the lysosomal enzyme activities considerably. A different lysosomal response to equal food supply was gained after deviding the cow stock into different groups regarding performance at a different lactation status. Growth, breed, age, capacity of food intake and milk performance might be influencing factors.

scholarly journals Extracellular Enzyme Activity and Microbial Diversity Measured on Seafloor Exposed Basalts from Loihi Seamount Indicate the Importance of Basalts to Global Biogeochemical Cycling

2014 ◽  
Vol 80 (16) ◽  
pp. 4854-4864 ◽  
Author(s):  
Myrna E. Jacobson Meyers ◽  
Jason B. Sylvan ◽  
Katrina J. Edwards
Keyword(s):  
Enzyme Activity ◽  
Microbial Communities ◽  
Enzyme Activities ◽  
Leucine Aminopeptidase ◽  
Extracellular Enzyme ◽  
Basaltic Rock ◽  
Rrna Gene ◽  
Content Type ◽  
Shelf Sediments ◽  
Potential Enzyme Activity

ABSTRACTSeafloor basalts are widely distributed and host diverse prokaryotic communities, but no data exist concerning the metabolic rates of the resident microbial communities. We present here potential extracellular enzyme activities of leucine aminopeptidase (LAP) and alkaline phosphatase (AP) measured on basalt samples from different locations on Loihi Seamount, HI, coupled with analysis of prokaryotic biomass and pyrosequencing of the bacterial 16S rRNA gene. The community maximum potential enzyme activity (Vmax) of LAP ranged from 0.47 to 0.90 nmol (g rock)−1h−1; theVmaxfor AP was 28 to 60 nmol (g rock)−1h−1. TheKmof LAP ranged from 26 to 33 μM, while theKmfor AP was 2 to 7 μM. Bacterial communities on Loihi basalts were comprised primarily ofAlpha-,Delta-, andGammaproteobacteria,Bacteroidetes, andPlanctomycetes. The putative ability to produce LAP is evenly distributed across the most commonly detected bacterial orders, but the ability to produce AP is likely dominated by bacteria in the ordersXanthomonadales,Flavobacteriales, andPlanctomycetales. The enzyme activities on Loihi basalts were compared to those of other marine environments that have been studied and were found to be similar in magnitude to those from continental shelf sediments and orders of magnitude higher than any measured in the water column, demonstrating that the potential for exposed basalts to transform organic matter is substantial. We propose that microbial communities on basaltic rock play a significant, quantifiable role in benthic biogeochemical processes.

CYCLISCHE SCHWANKUNGEN DER AKTIVITÄTEN VON HYDROXYSTEROID-DEHYDROGENASEN IM CORPUS LUTEUM DES RINDES

1972 ◽  
Vol 69 (2) ◽  
pp. 369-384
Author(s):  
H. Brandau ◽  
L. Brandau ◽  
G. Mutzke
Keyword(s):  
Enzyme Activity ◽  
Corpus Luteum ◽  
Enzyme Activities ◽  
Optical Method ◽  
Activity Patterns ◽  
Hydroxysteroid Dehydrogenase ◽  
Corpora Lutea ◽  
Bovine Corpus Luteum ◽  
Glucose 6 Phosphate Dehydrogenase

ABSTRACT In the bovine corpora lutea periodical activities of the Δ53β-, 3β-, 17β-and 20β-hydroxysteroid dehydrogenase (OHSDH) as well as activities of glyceraldehyde-3-phosphate- and glucose-6-phosphate dehydrogenase were measured quantitatively and the alterations throughout the different stages of the cycle were studied. After homogenization of the tissue and fractionate centrifugation the enzyme activities were determined by a standardized optical method. The activities of the Δ53β-, and 3β- and 17β-OHSDH increase slowly during the first 7 days of the cycle, the maximum is reached abruptly on the 12th to 13th day of the cycle. After a striking reduction the activities decline continually to the 19th to 21st day reaching the values detected at the beginning of the cycle. The 20β-OHSDH increases slowly to the maximum on the 15th day of the cycle. Activities of the 3α-OHSDH were obtained only inconsistently. The behaviour of the activities of G6PDH was nearly identical with that of the 3β-OHSDH, while the GAPDH shows only little fluctuations of its activities. The obtained enzyme activity patterns of the maturating and high functional corpus luteum correspond to the well-known data of the biosynthetic function of the bovine corpus luteum. The changes of the amounts of progesterone and 20β-progesterol agree with the course of the activities of the 3β- resp. 20β-OHSDH.

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