scholarly journals Enhancing the compost maturation of swine manure and rice straw by applying bioaugmentation

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Wei-Kuang Wang ◽  
Chih-Ming Liang
Keyword(s):  
Enzyme Activity ◽  
Carbon Source ◽  
Phanerochaete Chrysosporium ◽  
Bacillus Licheniformis ◽  
Enzyme Activities ◽  
Swine Manure ◽  
Bacterial Isolates ◽  
Manure Compost ◽  
Maturation Rate ◽  
Source Concentration

AbstractMicroorganisms capable of decomposing cellulose, xylan, starch and protein were individually isolated from swine manure compost and soil in this study. The correlations with pH, carbon source concentration, C/N ratio and enzyme activity among these isolated microorganisms were also investigated. Furthermore, the effect of additional inoculation in the compost was studied by measuring variations in the C/N ratio, enzyme activity and compost maturation rate. The inoculated microorganisms used in this study included four bacterial isolates and one commercial microorganism Phanerochaete chrysosporium. The results indicated that the isolated Kitasatospora phosalacinea strain C1, which is a cellulose-degraded microorganism, presented the highest enzyme activity at 31 ℃ and pH 5.5, while the C/N ratio was 0.8%. The isolated xylan-degraded microorganism Paenibacillus glycanilyticus X1 had the highest enzyme activity at 45 ℃ and pH 7.5, while the C/N ratio was 0.5%. The starch-degraded microorganism was identified as Bacillus licheniformis S3, and its highest enzyme activities were estimated to be 31 ℃ and pH 7.5 while the C/N ratio was 0.8%. The highest enzyme activity of the protein-degraded microorganism Brevinacillus agri E4 was obtained at 45 ℃ and pH 8.5, while the C/N ratio was 1.0%. The rate of temperature increase in the compost inoculated with P. chrysosporium was only higher than that of the compost without inoculation, and its compost maturation level was also lower than that of other composts with additional inoculation. The optimal initial C/N ratio of the compost was 27.5 and the final C/N ratio was 18.9. The composting results also indicated that the secondary inoculation would benefit compost maturation, and the lowest final C/N ratio of 17.0 was obtained.

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.

Identification of novel horA-harbouring bacteria capable of spoiling beer

2008 ◽  
Vol 54 (4) ◽  
pp. 321-325 ◽  
Author(s):  
Monique Haakensen ◽  
Barry Ziola
Keyword(s):  
Drug Resistance ◽  
Bacillus Cereus ◽  
Bacillus Licheniformis ◽  
Staphylococcus Epidermidis ◽  
Multi Drug Resistance ◽  
Bacterial Isolates ◽  
First Finding ◽  
Spoilage Bacteria ◽  
Beer Spoilage ◽  
Respective Species

An ATP-binding cassette (ABC) multi-drug resistance (MDR) gene was found in 4 Gram-positive bacterial isolates of environmental origin and found capable of spoiling beer. The bacteria isolated were Bacillus cereus , Bacillus licheniformis , Paenibacillus humicus , and Staphylococcus epidermidis ; all of which were previously unappreciated as beer-spoilage bacteria. The MDR gene found in these bacteria has less than 37% similarity to known ABC MDR proteins described for Bacillus and Staphylococcus , and this is the first finding of an ABC MDR gene in the genus Paenibacillus . The sequenced region of the gene was translated and compared phylogenetically with the closest GenBank matches of the respective species and the closest GenBank matches overall. The ABC MDR proteins from these isolates were found to cluster among known sequences of HorA, sharing 99.5% identity within the sequenced region. In the beer-spoilage-associated genera Lactobacillus and Pediococcus , the presence of the MDR gene horA correlates with the ability to grow in beer. As the unique horA-harbouring isolates described here are capable of growing in beer, it is likely that the presence of the horA gene likewise confers hop resistance to these organisms.

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 Aktivitas Bakteri Kitinolitik dari Cangkang Perna viridis sebagai Antifungi Phytophthora palmivora Penyebab Penyakit Busuk Buah Kakao (Theobroma cacao L.)

bionature ◽  
2018 ◽  
Vol 18 (2) ◽  
Author(s):  
Ulfia Nurul Khikmah ◽  
Muhson Isroni Isroni ◽  
Anisa Maulidiya
Keyword(s):  
Enzyme Activity ◽  
Phytophthora Palmivora ◽  
Perna Viridis ◽  
Bacterial Isolates ◽  
Chitinolytic Enzyme ◽  
Chitinolytic Bacteria ◽  
Agriculture Sector ◽  
Rot Disease ◽  
Bacterial Characterization ◽  
Physiological Characters

Abstract. The emphasis on the growth of Phytophthora palmivora was important in order to reduce Pod Rot Disease of cacao (Theobrorna cacao L.) which could harm agriculture sector. Some bacteria had chitinolytic enzyme activity that is potentially used as an antifungal against Phytophthora palmivora, because the cell wall of the fungi composed of chitin. The purpose of this research was to know chitinolytic bacteria from Perna viridis shell which had higher activity of chitinase enzyme, the amount of chitinase enzyme activity of each selected isolate, and to know the effect of chitinolytic bacterial isolates from Perna viridis shell to reduce the growth of Phytophthora palmivora. The bacteria were isolated from Perna viridis shell at Depok Beach, Kretek, Bantul, Yogyakarta. This research was an explorative research which include bacterial characterization and experimental research which include antagonistic test of chitinolytic bacteria against Phytophthora palmivora. The chitinolytic bacteria was isolated using selective chitin agar medium by pour plate method and then screening the isolates that had chitinase enzyme activity by measuring the enzyme activity of each bacterial isolates by spectrophotometric method. Selected bacterial isolates were characterized by macroscopic, microscopic and physiological characters. The bacteria that had been selected tested for their ability to reduce the growth of Phytophthora palmivora by Kirby Bauer modification method. The result showed that there were 10 isolates that had chitinase enzyme activity which two selected isolates had the higher chitinase enzyme activity. There were 7D and 6B isolates. The isolate 7D had 1,258 u/ml chitinase enzyme activity and isolate 6B had 1,212 u/ml chitinase enzyme activity. The result of chitinolytic bacterial antagonist test on Phytophthora palmivora growth showed that both bacterial isolates were potential to antifungal Phytophthora palmivora and showed a real effect in inhibiting the growth of Phytophthora palmivora with significance value < 0,05.Keywords: Chitinolytic Bacteria, Perna viridis, Phytophthora palmivora

scholarly journals Effects of supplementation with phosphorus, calcium and manganese during oil palm frond fermentation by Phanerochaete chrysosporium on ligninase enzyme activity

2020 ◽  
Vol 21 (5) ◽  
Author(s):  
Roni Pazla ◽  
Novirman Jamarun ◽  
Fauzia Agustin ◽  
Mardiati Zain ◽  
Arief Arief ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Phanerochaete Chrysosporium ◽  
Oil Palm ◽  
Manganese Peroxidase ◽  
Crude Protein ◽  
Lignin Degradation ◽  
Lignin Content ◽  
Oil Palm Frond ◽  
Range Test ◽  
Palm Frond

Abstract. Pazla R, Jamarun N, Agustin F, Zain M, Cahyani NO. 2020. Effects of supplementation with phosphorus, calcium and manganese during oil palm frond fermentation by Phanerochaete chrysosporium on ligninase enzyme activity. Biodiversitas 21: 1833-1838. The objective of this study was to evaluate the effects of supplementation with phosphorus (P) in combination with calcium (Ca) and manganese (Mn) during oil palm frond (OPF) fermentation by Phanerochaete chrysosporium on ligninase enzyme activity and lignin degradation. This study was carried out using a randomized complete design with 3 treatments (addition of P, Ca and Mn) and 5 replicates. The following treatments were performed: T1 (P 1000 + Ca 2000 + Mn 150 ppm), T2 (P 1500 + Ca 2000 + Mn 150 ppm), and T3  (P 2000 + Ca 2000 +Mn 150 ppm). The data were subjected to an analysis of variance (ANOVA), and differences between treatment means were tested using Duncan's multiple range test (DMRT). The parameters measured were as follows: lignin peroxidase (LiP) activity (U/mL), manganese peroxidase (MnP) activity (U/mL), crude protein (CP) content (%), crude fiber (CF) content (%) and the decrease in lignin (%). The results revealed a significant increase in LiP activity and CP content and a decrease in the lignin content (p<0.05) by the addition of P in the T3 treatment. However, the treatment nonsignificantly increased (p>0.05) MnP activity and significantly decreased (P<0.05) the CF content. In conclusion, supplementation of the OPF fermentation process with P 2000, Ca 2000, and Mn 150 ppm resulted in the highest ligninase enzyme activity and in decreased lignin content.

scholarly journals Lignolytic Enzyme Activity of Isolated Bacteria from Termite (Coptotermes Sp.) and Milkfish (Chanos chanos Forsskal, 1775) Guts

2021 ◽  
Vol 13 (1) ◽  
pp. 70-76
Author(s):  
Emi Latifah ◽  
Putri Dwi Mulyani ◽  
Yekti Asih Purwestri
Keyword(s):  
Enzyme Activity ◽  
Bacillus Licheniformis ◽  
Test Method ◽  
Chanos Chanos ◽  
Enzyme Isolation ◽  
Optimum Ph ◽  
Qualitative Test ◽  
Pseudomonas Alcaligenes ◽  
Enzyme Source ◽  
Brevibacillus Parabrevis

Bacteria BSR 2, Pseudomonas alcaligenes (BSR 3), Brevibacillus parabrevis (BSR 8), Brevibacillus sp. (BSR 9), isolated from termite gut and Bacillus licheniformis (BSA B1) isolated from milkfish gut have been known to possess celluloytic activity. However, their lignolytic ability has not been known. This study aimed to determine the lignolytic ability of bacteria isolated from termit (Coptotermes sp.) and milkfish (Chanos chanos Forsskal, 1775) guts and their enzymes characterization. The qualitative test was done through the spot test method, while quantitative assay was performed spectrophotometrically at 335 nm to calculate vanillin concentration. The isolates were grown in Lignin Mineral Medium, then the optical density (OD620) were measured every 24 hours for 5 days using spectrophotometer to determine their growth profile and the best isolation time of the lignolytic enzyme. Based on results, the best lignolytic enzyme isolation time for strains Bacillus licheniformis (BSA B1) and BSR 2 were 5 days, yielding lignolytic enzyme activity of 0.961 ± 0.168 U/mg and 2.176 ± 0.088 U/mg respectively,  while strains Pseudomonas alcaligenes (BSR 3), Brevibacillus parabrevis (BSR 8), and Brevibacillus sp. (BSR 9) were 4 days, yielding of 1.206 ± 0.045 U/mg, 1.162 ± 0.191 U/mg, and 0.896 ± 0.108 U/mg, respectively. The strain BSR 2 showed the highest lignolytic activity compared to other strains. The optimum temperature for lignolytic enzyme activity of BSR 2 was 30 ℃ and the optimum pH was 7. The lignolytic enzyme activity showed that these bacterial isolates can be a chance to be used as new alternative lignolytic enzyme source in commercial bioconversion process.

scholarly journals Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized

2009 ◽  
Vol 3 (2) ◽  
pp. 41-52
Author(s):  
Rasha T. Abdullah ◽  
Abdulkareem J. Hashim ◽  
JASIM M. Karhout
Keyword(s):  
Enzyme Activity ◽  
Bovine Serum Albumin ◽  
Ion Exchange ◽  
Bacillus Licheniformis ◽  
Enzyme Characterization ◽  
Optimal Temperature ◽  
Chicken Feathers ◽  
Local Isolate ◽  
Cellulose Column ◽  
Optimal Ph

The keratinase produced from local isolate Bacillus licheniformis was purified by two steps included precipitation by ammonium sulphate with 40% saturation; followed by ion exchange using CM-Cellulose column. The enzyme was purified to 12.6 times in the last step with an enzyme yield of 17%. Enzyme characterization results indicated that: The optimal pH for enzyme activity was 7.5 and it was stable at 7-9.5. The optimal temperature for enzyme activity was 50°C and it was stable for 30 min at 25-45 °C. Substrate specifity was tested using casein, Bovine serum albumin, gelatin, hooves, human hair, chicken feathers and wool; higher specifity was recorded using casein gave 0.6 unit /ml. The enzyme was inhibited by PMSF and metal ions like Hg+2, Fe+2, Cu+2 and Mn+2, and activated by Ca+2, Mg+2, Zn+2and Al+3.

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