scholarly journals Exploration of Amylases Producing Competency of Helicoverpa armigera Gut Bacterial Strain, Bacillus subtilis RTSBA6 6.00

2019 ◽  
Vol 3 (1) ◽  
pp. 75-79
Author(s):  
Ashok A. Shinde ◽  
Faiyaz K. Shaikh ◽  
Manvendra S. Kachole
Keyword(s):  
Bacillus Subtilis ◽  
Helicoverpa Armigera ◽  
Bacterial Strain ◽  
Bacterial Communities ◽  
Amylase Activity ◽  
Insect Pest ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Agar Plate ◽  
Helicoverpa Armígera

The Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) is a polyphagous insect pest of agriculturally important crops. The alkaline gut of this insect pest possesses diverse bacterial communities which may assist in digestive physiology. As part our investigations of understanding the role of gut bacterial communities in insect gut, here amylase producing competency of earlier identified H. armigera gut bacterial strain, i.e., Bacillus subtilis RTSBA6 6.00 is reported. Initial screening for amylase activity was assessed by starch agar plate. Upon 7% sodium dodecyl sulfate polyacrylamide gel electrophoresis amylase zymography, bacterial culture supernatant produced seven amylase bands on the gel. The observed molecular weights of amylases were 191.2 KDa, 158.0 KDa, 131.7 KDa, 54.0 KDa, 31.3 KDa, 67.2 KDa, and 44.6 KDa, respectively. Considerable amylase activity was observed in neutral to alkaline pH with optimum at pH 6.8. The optimal activity temperature of amylases was found to be 50°C, and the activity decreased dramatically at temperatures above 75°C.

scholarly journals Proteomics Analysis of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus Identified Two New Occlusion-Derived Virus-Associated Proteins, HA44 and HA100

2007 ◽  
Vol 81 (17) ◽  
pp. 9377-9385 ◽  
Author(s):  
Fei Deng ◽  
Ranran Wang ◽  
Minggang Fang ◽  
Yue Jiang ◽  
Xushi Xu ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Structural Proteins ◽  
Proteomics Analysis ◽  
Group I ◽  
Associated Proteins ◽  
Helicoverpa Armígera ◽  
Group Ii ◽  
First Time

ABSTRACT Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry were used to analyze the structural proteins of the occlusion-derived virus (ODV) of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV), a group II NPV. Twenty-three structural proteins of HearNPV ODV were identified, 21 of which have been reported previously as structural proteins or ODV-associated proteins in other baculoviruses. These include polyhedrin, P78/83, P49, ODV-E18, ODV-EC27, ODV-E56, P74, LEF-3, HA66 (AC66), DNA polymerase, GP41, VP39, P33, ODV-E25, helicase, P6.9, ODV/BV-C42, VP80, ODV-EC43, ODV-E66, and PIF-1. Two proteins encoded by HearNPV ORF44 (ha44) and ORF100 (ha100) were discovered as ODV-associated proteins for the first time. ha44 encodes a protein of 378 aa with a predicted mass of 42.8 kDa. ha100 encodes a protein of 510 aa with a predicted mass of 58.1 kDa and is a homologue of the gene for poly(ADP-ribose) glycohydrolase (parg). Western blot analysis and immunoelectron microscopy confirmed that HA44 is associated with the nucleocapsid and HA100 is associated with both the nucleocapsid and the envelope of HearNPV ODV. HA44 is conserved in group II NPVs and granuloviruses but does not exist in group I NPVs, while HA100 is conserved only in group II NPVs.

scholarly journals In-Plant Insect-Proofing by Trans-Kingdom RNAi

Proceedings ◽  
2020 ◽  
Vol 36 (1) ◽  
pp. 75
Author(s):  
Bally ◽  
Fishilevich ◽  
Campos ◽  
German ◽  
Narva ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Insect Pest ◽  
Cotton Bollworm ◽  
Wide Range ◽  
Helicoverpa Armígera

Helicoverpa armigera, the cotton bollworm, is a major insect pest for a wide range of agriculturalcrops. [...]

scholarly journals The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins

1983 ◽  
Vol 209 (2) ◽  
pp. 561-564 ◽  
Author(s):  
A R Orlando ◽  
P Ade ◽  
D Di Maggio ◽  
C Fanelli ◽  
L Vittozzi
Keyword(s):  
Bacillus Subtilis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Alpha Amylase ◽  
Wheat Protein ◽  
Wheat Proteins ◽  
Maximal Inhibition ◽  
Molecular Weights ◽  
Amylase Inhibitors

A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.

scholarly journals Proteomic Analysis of the Spore Coats of Bacillus subtilis and Bacillus anthracis

2003 ◽  
Vol 185 (4) ◽  
pp. 1443-1454 ◽  
Author(s):  
Erh-Min Lai ◽  
Nikhil D. Phadke ◽  
Maureen T. Kachman ◽  
Rebecca Giorno ◽  
Santiago Vazquez ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Bacillus Anthracis ◽  
Proteomic Analysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Detection Methods ◽  
Coat Proteins ◽  
Bona Fide ◽  
Spore Proteins ◽  
Spore Coat Proteins

ABSTRACT The outermost proteinaceous layer of bacterial spores, called the coat, is critical for spore survival, germination, and, for pathogenic spores, disease. To identify novel spore coat proteins, we have carried out a preliminary proteomic analysis of Bacillus subtilis and Bacillus anthracis spores, using a combination of standard sodium dodecyl sulfate-polyacrylamide gel electrophoresis separation and improved two-dimensional electrophoretic separations, followed by matrix-assisted laser desorption ionization-time of flight and/or dual mass spectrometry. We identified 38 B. subtilis spore proteins, 12 of which are known coat proteins. We propose that, of the novel proteins, YtaA, YvdP, and YnzH are bona fide coat proteins, and we have renamed them CotI, CotQ, and CotU, respectively. In addition, we initiated a study of coat proteins in B. anthracis and identified 11 spore proteins, 6 of which are candidate coat or exosporium proteins. We also queried the unfinished B. anthracis genome for potential coat proteins. Our analysis suggests that the B. subtilis and B. anthracis coats have roughly similar numbers of proteins and that a core group of coat protein species is shared between these organisms, including the major morphogenetic proteins. Nonetheless, a significant number of coat proteins are probably unique to each species. These results should accelerate efforts to develop B. anthracis detection methods and understand the ecological role of the coat.

Purification and characterization of the extracellular α-amylase activity of the yeast Schwanniomyces alluvius

1987 ◽  
Vol 65 (10) ◽  
pp. 899-908 ◽  
Author(s):  
F. Moranelli ◽  
M. Yaguchi ◽  
G. B. Calleja ◽  
A. Nasim
Keyword(s):  
Amino Acid ◽  
Amylase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
Proteinase K ◽  
Ph Optimum ◽  
Sds Page

The extracellular α-amylase activity of the yeast Schwanniomyces alluvius has been purified by anion-exchange chromatography on DEAE-cellulose and gel-filtration chromatography on Sephadex G-100. Sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE) and N-terminal amino acid analysis of the purified sample indicated that the enzyme preparation was homogeneous. The enzyme is a glycoprotein having a molecular mass of 52 kilodaltons (kDa) estimated by SDS–PAGE and 39 kDa by gel filtration on Sephadex G-100. Chromatofocusing shows that it is an acidic protein. It is resistant to trypsin but sensitive to proteinase K. Its activity is inhibited by the divalent cation chelators EDTA and EGTA and it is insensitive to sulfhydryl-blocking agents. Exogenous divalent cations are inhibitory as are high concentrations of monovalent salts. The enzyme has a pH optimum between 3.75 and 5.5 and displays maximum stability in the pH range of 4.0–7.0. Under the conditions tested, the activity is maximal between 45 and 50 °C and is very thermolabile. Analysis of its amino acid composition supports its acidic nature.

scholarly journals Evaluation of toxicological responses of Helicoverpa armigera (Hübner) against some insecticides by using probit analysis in laboratory

2019 ◽  
Vol 3 (1) ◽  
Author(s):  
Shafia Saba ◽  
Madiha Mobeen Khan ◽  
Imran Akhtar ◽  
Syed Waqar Hussain Shah ◽  
Naeem Arshad Maan ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Insect Pest ◽  
Probit Analysis ◽  
Comparative Efficacy ◽  
Lc50 Value ◽  
Helicoverpa Armígera ◽  
Helicoverpa Armigera Hubner

The present study was designed to determine the LC50 of some insecticides commonly used against Helicoverpa armigera and their comparative efficacy against the insect pest. The second instar larvae of H. armigera reared in the laboratory were selected for leaf dip bioassay. Two types of insecticides viz. conventional (deltamethrin and bifenthrin) and new chemistry (spinosad and indoxacarb) were assessed in the present studies. The results revealed that bifenthrin was more toxic to the second instar larvae of H. armigera at all the doses with lower LC50 value of 120.007 ppm as compared to deltamethrin with the highest LC50 value of 292.404 ppm. Among the new chemistry insecticides, indoxacarb proved to be more toxic than spinosad with LC50 of 5.592 ppm. LC50 of spinosad was 8.201 ppm showing 1.46 times less toxicity than indoxacarb.

scholarly journals Forecasting Helicoverpa armigera (Lepidoptera: Noctuidae) larval phenology in pigeonpea and chickpea crops using growing degree days

2021 ◽  
Vol 22 (3) ◽  
pp. 320-331
Author(s):  
B. KIRAN GANDHI ◽  
S.K. SINGH ◽  
KRISHNA KUMAR ◽  
S. VENNILA ◽  
Y. SRUJANA ◽  
...  
Keyword(s):  
Logistic Regression ◽  
Regression Model ◽  
Helicoverpa Armigera ◽  
Logistic Regression Model ◽  
Management Practices ◽  
Insect Pest ◽  
Economic Losses ◽  
Economic Damage ◽  
Incidence Data ◽  
Helicoverpa Armígera

Gram pod borer, Helicoverpa armigera is a serious insect pest of pigeonpea and chickpea crops, responsible for huge economic losses. Timely forecasting and subsequent sensible management practices of H. armigera would save the crops from economic damage. In the present study, H. armigera larval incidence data was recorded from sixteen pigeonpea and chickpea growing locations (Maharashtra, India) for three seasons (2015, 2016 and 2017). Observed accumulated GDD (from 40 SMW to 7 SMW) revealed, H. armigera completed one generation in 29 days to develop 4 generations across the locations and seasons. After accumulating 86GDD (40 SMW) and 62 GDD (43 SMW), larval ‘biofix’ (initial incidence of larvae) was started in pigeonpea and chickpea, respectively. Logistic regression model estimated accumulated GDD required by H. armigera larvae to reach ETL in pigeonpea (629 GDD) and chickpea (378 GDD), which was same as observed accumulated GDD. Statistical criteria viz., Adjusted r2, AIC and BIC projected logistic regression model as a better performer in most cases. The geographically unique models developed based on biofix and accumulated GDD in this study can be used for timely advisories and sustainable management of H. armigera in pigeonpea and chickpea crops after field validation.

scholarly journals Changes in α- and ß-amylase during Storage of Sweetpotato Lines with Varying Starch Hydrolysis Potential

1993 ◽  
Vol 118 (2) ◽  
pp. 236-242 ◽  
Author(s):  
Teresa A. Morrison ◽  
Russell Pressey ◽  
Stanley J. Kays
Keyword(s):  
Reducing Sugars ◽  
Amylase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Storage Period ◽  
Total Sugar ◽  
Starch Hydrolysis ◽  
Storage Root ◽  
High Starch ◽  
Low Levels

Staple-type lines of sweetpotato [Ipomoea batatus (L.) Lam.] do not sweeten significantly upon cooking as compared to the traditional-type lines. Four lines exhibiting distinct differences in sweetness after cooking were evaluated for changes in α- and ß-amylase activity and reducing sugars (by HPLC) at harvest, after curing, and at intervals during 180 days of storage. The traditional cultivar `Jewel' and staple-type line `Sumor' displayed high a- and ß-amylase activities, which rose from low levels at harvest to peak levels ≈ 90 days into the storage period. Staple-type lines `99' and `86' displayed significantly lower a- and ß-amylase activities. By using polyclonal sweetpotato ß-amylase antibody and western blot following native- and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it was confirmed that a lower level of ß-amylase synthesis existed in `99' and `86'. Quantitatively, `Jewel', `Sumor', and an additional staple-type line, `HiDry', had 361,374, and 365 μg ß-amylase protein per gram of fresh storage root tissue, respectively, while `99' and `86' possessed <60 and 12 μg·g-1, respectively. In raw roots, individual (glucose, fructose, and sucrose) and total sugar concentrations were significantly higher in `Jewel' than in `Sumor', `99', or `86'. Only trace amounts of maltose were found in raw roots of any line. Sucrose, glucose, and fructose concentrations decreased with baking in all lines except `86', in which they increased. There was substantial maltose produced by baking `Jewel' and `Sumor', but only trace amounts found in baked `99' and `86'. Sweetpotato germplasm can be separated into four general classes based on initial sugar concentration and changes during cooking: 1) low sugars/low starch hydrolysis, 2) low sugars/high starch hydrolysis, 3) high sugars/low starch hydrolysis, and 4) high sugars/high starch hydrolysis. At least two mechanisms may confer the lack of starch hydrolysis and subsequent sweetening in staple-type sweetpotato: 1) inhibition of ß-amylase synthesis, and 2) a nonenzyme mediated mechanism.

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