Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100408
R. Ramu, Prithvi S Shirahatti, Deepika Th, Shrisha Naik Bajpe, Navya Sreepathi, Shashank M. Patil, N. Mn
Banana pseudostem is attributed as a potent food source that serves as a health promoter as well as an ethnopharmacological agent in Indian medicine system. The aim of this investigation was to examine the anti- diabetic activity of banana pseudostem ethanol extract (EE), Stigmasterol (C1), and β -Sitosterol (C2) obtained from EE. The in vitro studies against α -glucosidase enzyme was evaluated for C1 and C2 (IC 50 values of 7.31 ± 0.12 and 7.80 ± 0.93 µ g/ml, respectively) which revealed a mixed type inhibition and entailed two inhibition constants viz., K 1 and K 2 . In vitro glycation experiments further revealed that EE, and its components inhibited each stage of protein glycation as well as the generation of intermediate chemicals. EE, C1 and C2 inhibited aldose reductase potently, with IC 50 values of 2.67 ± 0.27, 1.80 ± 0.36, and 1.93 ± 0.37 g/ml, respectively. In vivo studies on the diabetic complications known as hypercholesterolemia and hypertriacylglycerolemia in diabetic rat models also revealed significant improvements in serum/liver levels as well as a notable increase in the activities of enzymatic and non-enzymatic antioxidant levels. In conclusion, EE has the potential to be an important therapeutic component in the treatment of diabetes and its complications.
{"title":"Investigating Musa paradisiaca (Var. Nanjangud rasa bale) pseudostem in preventing hyperglycemia along with improvement of diabetic complications","authors":"R. Ramu, Prithvi S Shirahatti, Deepika Th, Shrisha Naik Bajpe, Navya Sreepathi, Shashank M. Patil, N. Mn","doi":"10.7324/jabb.2022.100408","DOIUrl":"https://doi.org/10.7324/jabb.2022.100408","url":null,"abstract":"Banana pseudostem is attributed as a potent food source that serves as a health promoter as well as an ethnopharmacological agent in Indian medicine system. The aim of this investigation was to examine the anti- diabetic activity of banana pseudostem ethanol extract (EE), Stigmasterol (C1), and β -Sitosterol (C2) obtained from EE. The in vitro studies against α -glucosidase enzyme was evaluated for C1 and C2 (IC 50 values of 7.31 ± 0.12 and 7.80 ± 0.93 µ g/ml, respectively) which revealed a mixed type inhibition and entailed two inhibition constants viz., K 1 and K 2 . In vitro glycation experiments further revealed that EE, and its components inhibited each stage of protein glycation as well as the generation of intermediate chemicals. EE, C1 and C2 inhibited aldose reductase potently, with IC 50 values of 2.67 ± 0.27, 1.80 ± 0.36, and 1.93 ± 0.37 g/ml, respectively. In vivo studies on the diabetic complications known as hypercholesterolemia and hypertriacylglycerolemia in diabetic rat models also revealed significant improvements in serum/liver levels as well as a notable increase in the activities of enzymatic and non-enzymatic antioxidant levels. In conclusion, EE has the potential to be an important therapeutic component in the treatment of diabetes and its complications.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"10 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"129954524","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100416
K. Choudhury, N. Chakraborty, M. Gandhi, S. Chatterjee, R. Purty
Rheumatoid arthritis (RA) and Sjögren’s syndrome (SS) are chronic, autoimmune diseases characterized by loss of mobility, pain, and inflammation around the major joints and dysfunctional exocrine glands, respectively. In the present study, the microarray gene expression data in the whole blood of RA (Accession No. GSE93272) and SS patients (Accession No. GSE84844) were used in the identification of differentially expressed genes (DEGs) and pathways involved in RA and SS using computational approaches. DEGs associated with fold change (Log2FC±1.0) were found in 206 genes in RA and 138 genes in SS. Between both the datasets, 46 genes were expressed commonly in both RA and SS. The Log2FC filtered DEGs were further used for comparative gene expression analysis, gene ontology, and pathway enrichment analysis. The investigations revealed crucial genes and pathways that are involved in both RA and SS pathophysiology and deeper analysis of these pathways gives an insight into the progression and involvement of both diseases.
{"title":"Comparative transcriptome analysis to identify common genes involved in the progression of Sjögren’s syndrome and rheumatoid arthritis","authors":"K. Choudhury, N. Chakraborty, M. Gandhi, S. Chatterjee, R. Purty","doi":"10.7324/jabb.2022.100416","DOIUrl":"https://doi.org/10.7324/jabb.2022.100416","url":null,"abstract":"Rheumatoid arthritis (RA) and Sjögren’s syndrome (SS) are chronic, autoimmune diseases characterized by loss of mobility, pain, and inflammation around the major joints and dysfunctional exocrine glands, respectively. In the present study, the microarray gene expression data in the whole blood of RA (Accession No. GSE93272) and SS patients (Accession No. GSE84844) were used in the identification of differentially expressed genes (DEGs) and pathways involved in RA and SS using computational approaches. DEGs associated with fold change (Log2FC±1.0) were found in 206 genes in RA and 138 genes in SS. Between both the datasets, 46 genes were expressed commonly in both RA and SS. The Log2FC filtered DEGs were further used for comparative gene expression analysis, gene ontology, and pathway enrichment analysis. The investigations revealed crucial genes and pathways that are involved in both RA and SS pathophysiology and deeper analysis of these pathways gives an insight into the progression and involvement of both diseases.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"221 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"116000837","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100403
Gururaj B. Tennalli, Soumya Garawadmath, Lisa Sequeira, Shreya Murudi, V. Patil, M. N. Divate, B. Hungund
The present study reports production, partial purification, and media optimization for alkaline protease using Bacillus cereus PW3A. A profiling study for protease production indicates maximum enzyme activity (17.22 U/ml) was observed after 48 h of incubation. The studies also showed that the enzyme activity increased with the decrease in carbon content indicating the growth associated with nature protease production. Partial purification of protease was done using ammonium sulfate precipitation and dialysis. Further studies were conducted to assess significant media ingredients influencing protease production using the one-factor-at-a-time approach and Plackett-Burman design. Fructose and yeast extract were identified as the most significant variables. Response surface methodology was applied to optimize the factors for maximizing protease production. The results showed that the production increased from 17.22 U/ml to 47.43 U/ml indicating a three-fold augment in enzyme activity. Characterization of protease showed that the highest enzyme activity was shown at pH 8.0 and temperature 50°C; however, significant enzyme activity was retained till pH 10 and temperature 60°C. Using casein as substrate, the enzyme showed maximum activity V max 39 U/ml and K m 18 μ M. The activity was enhanced by MgCl 2 and CuSO 4 and inhibited by HgCl 2 . Since the enzyme has both pH and temperature stability with greater substrate affinity, this protease finds many useful industrial applications.
{"title":"Media optimization for the production of alkaline protease by Bacillus cereus PW3A using response surface methodology","authors":"Gururaj B. Tennalli, Soumya Garawadmath, Lisa Sequeira, Shreya Murudi, V. Patil, M. N. Divate, B. Hungund","doi":"10.7324/jabb.2022.100403","DOIUrl":"https://doi.org/10.7324/jabb.2022.100403","url":null,"abstract":"The present study reports production, partial purification, and media optimization for alkaline protease using Bacillus cereus PW3A. A profiling study for protease production indicates maximum enzyme activity (17.22 U/ml) was observed after 48 h of incubation. The studies also showed that the enzyme activity increased with the decrease in carbon content indicating the growth associated with nature protease production. Partial purification of protease was done using ammonium sulfate precipitation and dialysis. Further studies were conducted to assess significant media ingredients influencing protease production using the one-factor-at-a-time approach and Plackett-Burman design. Fructose and yeast extract were identified as the most significant variables. Response surface methodology was applied to optimize the factors for maximizing protease production. The results showed that the production increased from 17.22 U/ml to 47.43 U/ml indicating a three-fold augment in enzyme activity. Characterization of protease showed that the highest enzyme activity was shown at pH 8.0 and temperature 50°C; however, significant enzyme activity was retained till pH 10 and temperature 60°C. Using casein as substrate, the enzyme showed maximum activity V max 39 U/ml and K m 18 μ M. The activity was enhanced by MgCl 2 and CuSO 4 and inhibited by HgCl 2 . Since the enzyme has both pH and temperature stability with greater substrate affinity, this protease finds many useful industrial applications.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"28 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122151374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100402
A. Márquez, Nayeli Soria- Calderón, M. G. Villa-Rivera, Everardo López- Romero, Nancy Calderón- Cortés
In this work we purified a polygalacturonase enzyme from the midgut of larvae of the xylophagous insect Oncideres albomarginata chamela . The polygalacturonase showed high enzymatic activity (390.7 U/mg) in the crude extract and was purified to apparent homogeneity by means of cation exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The molecular mass of the polygalacturonase was estimated to be 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had an optimum pH of 6.0 and an optimum temperature of 50°C. According to the kinetic studies on polygalacturonic acid, the polygalacturonase showed a Km of 3.18 mg/ml and Vmax of 716.15 U/mg. The enzymatic properties of the purified enzyme correspond to those reported for highly active commercially produced enzymes, highlighting the potential of this insect enzyme to be used in industrial applications.
{"title":"Purification and characterization of a polygalacturonase from the xylophagous insect Oncideres albomarginata chamela (Coleoptera: Cerambycidae)","authors":"A. Márquez, Nayeli Soria- Calderón, M. G. Villa-Rivera, Everardo López- Romero, Nancy Calderón- Cortés","doi":"10.7324/jabb.2022.100402","DOIUrl":"https://doi.org/10.7324/jabb.2022.100402","url":null,"abstract":"In this work we purified a polygalacturonase enzyme from the midgut of larvae of the xylophagous insect Oncideres albomarginata chamela . The polygalacturonase showed high enzymatic activity (390.7 U/mg) in the crude extract and was purified to apparent homogeneity by means of cation exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The molecular mass of the polygalacturonase was estimated to be 37 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme had an optimum pH of 6.0 and an optimum temperature of 50°C. According to the kinetic studies on polygalacturonic acid, the polygalacturonase showed a Km of 3.18 mg/ml and Vmax of 716.15 U/mg. The enzymatic properties of the purified enzyme correspond to those reported for highly active commercially produced enzymes, highlighting the potential of this insect enzyme to be used in industrial applications.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"64 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122809813","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100409
I. Udo, A. E. Uko, Ekemini Edet Obok, Jesam O. Ubi, S. Umoetok
The deleterious effect of salinity and root-knot nematodes on sweet pepper is enormous. A screenhouse experiment was conducted to evaluate the efficacy of three arbuscular mycorrhizal fungi (AMF) in alleviating adverse effects of salinity and M. incognita on sweet pepper. A 2 × 3 × 4 factorial experiment was laid out in a completely randomized design with three replications. The 24-treatment combinations were three mycorrhizal fungi ( Glomus mosseae , Glomus deserticola , and Gigaspora gigantea ), an uninoculated control, three salinity levels (0.16, 3.24, and 6.06 dS/m), and inoculation either with or without 5,000 eggs of M. incognita . The results showed that sweet pepper variety Tatase was highly susceptible to M. incognita infection with heavy galls on nonmycorrhizal plants. Nematode inoculation and salinity significantly ( P ≤ 0.05) impaired growth, AMF root colonization, and dry matter production compared with the control plants. Increase in salinity level significantly ( P ≤ 0.05) reduced root galling and egg mass production. AMF inoculation significantly ( P ≤ 0.05) reduced root galling and significantly enhanced growth and dry matter yield in the presence or absence of nematode infection at all salinity levels compared with the nonmycorrhizal plants. Among the AMF species, G . deserticola was the most efficient in ameliorating the injurious effects of salt and M. incognita .
{"title":"Management of Meloidogyne incognita and salinity on sweet pepper (Capsicum annuum L.) with different arbuscular mycorrhizal fungus species","authors":"I. Udo, A. E. Uko, Ekemini Edet Obok, Jesam O. Ubi, S. Umoetok","doi":"10.7324/jabb.2022.100409","DOIUrl":"https://doi.org/10.7324/jabb.2022.100409","url":null,"abstract":"The deleterious effect of salinity and root-knot nematodes on sweet pepper is enormous. A screenhouse experiment was conducted to evaluate the efficacy of three arbuscular mycorrhizal fungi (AMF) in alleviating adverse effects of salinity and M. incognita on sweet pepper. A 2 × 3 × 4 factorial experiment was laid out in a completely randomized design with three replications. The 24-treatment combinations were three mycorrhizal fungi ( Glomus mosseae , Glomus deserticola , and Gigaspora gigantea ), an uninoculated control, three salinity levels (0.16, 3.24, and 6.06 dS/m), and inoculation either with or without 5,000 eggs of M. incognita . The results showed that sweet pepper variety Tatase was highly susceptible to M. incognita infection with heavy galls on nonmycorrhizal plants. Nematode inoculation and salinity significantly ( P ≤ 0.05) impaired growth, AMF root colonization, and dry matter production compared with the control plants. Increase in salinity level significantly ( P ≤ 0.05) reduced root galling and egg mass production. AMF inoculation significantly ( P ≤ 0.05) reduced root galling and significantly enhanced growth and dry matter yield in the presence or absence of nematode infection at all salinity levels compared with the nonmycorrhizal plants. Among the AMF species, G . deserticola was the most efficient in ameliorating the injurious effects of salt and M. incognita .","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"66 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"129994317","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100410
Krishna P. Patel, S. Parikh
Lipase is an extracellular enzyme produced by various sources such as plants, animals, and microorganisms. Microorganisms are the best source of extracellular lipase and are used in various industrial processes for their potential application. In this research study, lipase producers were isolated in oil-contaminated soil collected from oil refineries of Aravalli district situated in Gujarat, India. It was screened on a selective medium like tributyrin agar. The isolate was identified using the 16S rRNA method and lipase enzyme activity was quantitatively assayed. Submerged fermentation was used for the production of lipase using olive oil as a substrate. Maximum lipase activity was found from Bacillus safensis . Lipase from B. safensis was purified using (NH 4 ) 2 SO 4 precipitation and ion exchange chromatography and characterized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis. B. safensis exhibited specific activity of 13.71 U/mg with a yield of 16.16% and the molecular weight of lipase is 55kDa was obtained.
{"title":"Identification, production, and purification of a novel lipase from Bacillus safensis","authors":"Krishna P. Patel, S. Parikh","doi":"10.7324/jabb.2022.100410","DOIUrl":"https://doi.org/10.7324/jabb.2022.100410","url":null,"abstract":"Lipase is an extracellular enzyme produced by various sources such as plants, animals, and microorganisms. Microorganisms are the best source of extracellular lipase and are used in various industrial processes for their potential application. In this research study, lipase producers were isolated in oil-contaminated soil collected from oil refineries of Aravalli district situated in Gujarat, India. It was screened on a selective medium like tributyrin agar. The isolate was identified using the 16S rRNA method and lipase enzyme activity was quantitatively assayed. Submerged fermentation was used for the production of lipase using olive oil as a substrate. Maximum lipase activity was found from Bacillus safensis . Lipase from B. safensis was purified using (NH 4 ) 2 SO 4 precipitation and ion exchange chromatography and characterized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis. B. safensis exhibited specific activity of 13.71 U/mg with a yield of 16.16% and the molecular weight of lipase is 55kDa was obtained.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"30 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"126637788","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100407
Grace Jadesola Oyinbogbola, M. Olaleye, Aanuoluwapo Ruth Adetuyi, I. Saliu, A. Akinmoladun
{"title":"Additive and antagonistic effects of selected polyphenols on biochemical indices of isoproterenol-induced toxicity in Wistar rats","authors":"Grace Jadesola Oyinbogbola, M. Olaleye, Aanuoluwapo Ruth Adetuyi, I. Saliu, A. Akinmoladun","doi":"10.7324/jabb.2022.100407","DOIUrl":"https://doi.org/10.7324/jabb.2022.100407","url":null,"abstract":"","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"171 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"116128314","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100405
Piyachat Wiriyaampaiwong, Chutima Karnmongkol, Arpaporn Punpad, Nattapong Srisamoot, Wutti Rattanavichai, Alongkod Tanomtong, S. Daduang, S. Klaynongsruang, A. Tankrathok
Cathelicidins, a group of vertebrate multifunctional molecules, play a role in innate immunity. In this study, a cathelicidin was identified from the lungs of frogs, Hoplobatrachus rugulosus . A 474 base pairs complementary DNA sequence encoded a 157 amino acid residue prepropeptide of H. rugulosus cathelicidin (cathelicidin-HR), which consisting of a 20-residue signal peptide sequence, a 108-residue cathelin region, and a 29-residue cathelicidin-HR peptide. Amino acid sequence alignment and cladogram analysis illustrated that cathelicidin-HR have a high degree of similarity to other amphibian cathelicidins. The cathelicidin-HR peptide displays very low antimicrobial activity but exhibits dose-dependent antioxidant activity. Moreover, this peptide expresses DNA damage inhibition against UV/H 2 O 2 -induction. The molecular docking indicated that DNA damage protection of cathelicidin-HR might occur via DNA-peptide complex formation. This is the first amphibian cathelicidin peptide that possesses DNA damage inhibitory activity which might play a crucial role in oxidative stress.
{"title":"Cathelicidin-HR from Hoplobatrachus rugulosus: an antioxidant peptide that performs a protective effect against UV/H2O2 -induced DNA damage","authors":"Piyachat Wiriyaampaiwong, Chutima Karnmongkol, Arpaporn Punpad, Nattapong Srisamoot, Wutti Rattanavichai, Alongkod Tanomtong, S. Daduang, S. Klaynongsruang, A. Tankrathok","doi":"10.7324/jabb.2022.100405","DOIUrl":"https://doi.org/10.7324/jabb.2022.100405","url":null,"abstract":"Cathelicidins, a group of vertebrate multifunctional molecules, play a role in innate immunity. In this study, a cathelicidin was identified from the lungs of frogs, Hoplobatrachus rugulosus . A 474 base pairs complementary DNA sequence encoded a 157 amino acid residue prepropeptide of H. rugulosus cathelicidin (cathelicidin-HR), which consisting of a 20-residue signal peptide sequence, a 108-residue cathelin region, and a 29-residue cathelicidin-HR peptide. Amino acid sequence alignment and cladogram analysis illustrated that cathelicidin-HR have a high degree of similarity to other amphibian cathelicidins. The cathelicidin-HR peptide displays very low antimicrobial activity but exhibits dose-dependent antioxidant activity. Moreover, this peptide expresses DNA damage inhibition against UV/H 2 O 2 -induction. The molecular docking indicated that DNA damage protection of cathelicidin-HR might occur via DNA-peptide complex formation. This is the first amphibian cathelicidin peptide that possesses DNA damage inhibitory activity which might play a crucial role in oxidative stress.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"52 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"116153291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100412
Hanan M. H. Ali, Dalia Abdel Halim M. Sallam
This study was conducted during the 2019/2020 and 2020/2021 seasons at the Farm of Medicinal and Aromatic Plants Research Department in El-Kanater El-Khairia to evaluate the effect of glycine and tryptophan, each of them alone, at concentrations of 50, 100, and 150 ppm on vegetative growth, fruit yield, oil production, and plant hormones of caraway plants ( Carum carvi L.). The results are summarized as follows: caraway plants showed a positive response to the foliar application by glycine and tryptophan. The plant that received tryptophan at 150 ppm has the highest vegetative growth, denoted as plant height and the number of branches/ plant, and produced the highest number of umbels per plant and fruit yield compared with other treatments in the two seasons. The high concentration of glycine or tryptophan (150 ppm) significantly increased the essential oil percentage compared to the control in both seasons. The application of tryptophan at a concentration of 150 ppm recorded the highest percentage of the main constituent of the essential oil (carvone). Moreover, it also affected some plant hormones such as gibberellin, indole acetic acid, and abscisic acid.
{"title":"Inducing the growth and flowering of caraway (Carum carvi L.) plant","authors":"Hanan M. H. Ali, Dalia Abdel Halim M. Sallam","doi":"10.7324/jabb.2022.100412","DOIUrl":"https://doi.org/10.7324/jabb.2022.100412","url":null,"abstract":"This study was conducted during the 2019/2020 and 2020/2021 seasons at the Farm of Medicinal and Aromatic Plants Research Department in El-Kanater El-Khairia to evaluate the effect of glycine and tryptophan, each of them alone, at concentrations of 50, 100, and 150 ppm on vegetative growth, fruit yield, oil production, and plant hormones of caraway plants ( Carum carvi L.). The results are summarized as follows: caraway plants showed a positive response to the foliar application by glycine and tryptophan. The plant that received tryptophan at 150 ppm has the highest vegetative growth, denoted as plant height and the number of branches/ plant, and produced the highest number of umbels per plant and fruit yield compared with other treatments in the two seasons. The high concentration of glycine or tryptophan (150 ppm) significantly increased the essential oil percentage compared to the control in both seasons. The application of tryptophan at a concentration of 150 ppm recorded the highest percentage of the main constituent of the essential oil (carvone). Moreover, it also affected some plant hormones such as gibberellin, indole acetic acid, and abscisic acid.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"95 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"126150423","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-06-01DOI: 10.7324/jabb.2022.100419
A. Padma, K. A. Kumar, P. Reddanna
Sheep uterine tissue is rich in the enzyme 5-lipoxygenase (5-LOX) that generates 5-hydroperoxyeicosatetraenoic acid (5-HPETE) on incubation with arachidonic acid (AA). The present study focuses on the ability of the enzyme 5-LOX to further act as 5, 6 leukotriene A4 (LTA 4 ) synthase using 5-HPETE as a substrate. On incubation of 5-LOX with 5-HPETE and analysis of products on reversed-phase high-performance liquid chromatography, a prominent peak with a characteristic conjugated triene peak having absorption maxima of 261, 271, and 281 nm appeared. Based on cochromatography, the peak was identified as 5(S), 6(S)-dihydroxyeicosatetraenoic acid (5[S], 6[S]-diHETE), the non-enzymatic product of 5, 6 LTA 4 . As the synthesis of 5,6-LTA 4 from 5-HPETE requires 8-LOX activity, the present study demonstrates the dual LOX, 5- and 8-LOX activity for uterine 5-LOX, that is, 5-,6- LTA 4 synthase in sheep uterus. In addition, endogenous 5,6-LTC 4 , the glutathione conjugate of 5,6-LTA 4 , was also observed in the sheep uterine homogenate, further demonstrating the synthesis of 5,6-LTA 4 in the sheep uterine tissue.
{"title":"Model for metabolism of arachidonic acid by 5-lipoxygenase as 5, 6-LTA4 synthase in the sheep uterus: Evidence from in vitro studies","authors":"A. Padma, K. A. Kumar, P. Reddanna","doi":"10.7324/jabb.2022.100419","DOIUrl":"https://doi.org/10.7324/jabb.2022.100419","url":null,"abstract":"Sheep uterine tissue is rich in the enzyme 5-lipoxygenase (5-LOX) that generates 5-hydroperoxyeicosatetraenoic acid (5-HPETE) on incubation with arachidonic acid (AA). The present study focuses on the ability of the enzyme 5-LOX to further act as 5, 6 leukotriene A4 (LTA 4 ) synthase using 5-HPETE as a substrate. On incubation of 5-LOX with 5-HPETE and analysis of products on reversed-phase high-performance liquid chromatography, a prominent peak with a characteristic conjugated triene peak having absorption maxima of 261, 271, and 281 nm appeared. Based on cochromatography, the peak was identified as 5(S), 6(S)-dihydroxyeicosatetraenoic acid (5[S], 6[S]-diHETE), the non-enzymatic product of 5, 6 LTA 4 . As the synthesis of 5,6-LTA 4 from 5-HPETE requires 8-LOX activity, the present study demonstrates the dual LOX, 5- and 8-LOX activity for uterine 5-LOX, that is, 5-,6- LTA 4 synthase in sheep uterus. In addition, endogenous 5,6-LTC 4 , the glutathione conjugate of 5,6-LTA 4 , was also observed in the sheep uterine homogenate, further demonstrating the synthesis of 5,6-LTA 4 in the sheep uterine tissue.","PeriodicalId":423079,"journal":{"name":"Journal of Applied Biology & Biotechnology","volume":"601 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132657932","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
京公网安备 11010802042870号
京ICP备2023020795号-1
扫码关注我们
求助内容：
应助结果提醒方式：