TITLE

Effect of Inhibitors from Plant Seeds on Digestive Proteolytic Activities in Larvae of the Date Palm Fruit Stalk Borer, Oryctes elegans Prell (Coleoptera: Scarabaeidae)

AUTHOR(S)
Riseh, N. Saberi; Ghadamyari, M.; Hosseinnaveh, V.; Moetamedinia, B.; Aghaali, N.
PUB. DATE
September 2014
SOURCE
Journal of Agricultural Science & Technology;Sep/Oct2014, Vol. 16 Issue 5, p981
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The date palm fruit stalk borer is one of the most important pests of date palm in the world. Biochemical properties of digestive proteases in Oryctes elegans Prell larvae were investigated in this research and optimal total proteolytic and trypsin activities were obtained at pH 9.0 and 11.0, respectively. Activity staining of protease on SDS-PAGE showed one isoform. Also, zymogram pattern of trypsin using nitro-cellulose membrane revealed two isoforms. The inhibitory effect of PMSF, TLCK, TPCK, EDTA, iodoacetate and iodoacetamide were determined on O. elegans proteolytic activity. The iodoacetamide showed the highest inhibition on total proteolytic activity. Therefore, cysteine protease accounted for the major proteases in the gut of O. elegans. Total proteolytic activity was inhibited 22.3 and .15% by inhibitors extracted from Vicia faba and Lathyrus sativus, respectively. However, the inhibitors extracted from seeds of Prosopis farcta, Panecum miliaceum, and Alhagi maurorum showed negligible inhibitory effects on proteolytic activities. Trypsin activity was inhibited 91.5 and 82.3% by inhibitors extracted from V. faba and L. sativus, respectively. Electrophoretic analysis showed that inhibitors extracted from V. faba reduced the intensity of total proteolytic and trypsin activities. The inhibitor from V. faba was purified by ammonium sulfate precipitation and gel-filtration, also the molecular mass of inhibitor was determined 35 kDa. This purified inhibitor was able to inhibit trypsin activity by 72.7%. In addition, the highest inhibition of trypsin activity by inhibitor from V. faba occurred at pH 11.0. Also, the stability of inhibitor from V. faba was evaluated at different pHs and temperatures. This inhibitor was stable at pH 11.0 and 30 °C.
ACCESSION #
111400987

 

Related Articles

  • Cold-active extracellular alkaline protease from an alkaliphilic Stenotrophomonas maltophilia: production of enzyme and its industrial applications. Kuddus, Mohammed; Ramteke, Pramod W. // Canadian Journal of Microbiology;Nov2009, Vol. 55 Issue 11, p1294 

    A novel psychro-tolerant bacterium Stenotrophomonas maltophilia (MTCC 7528) with an ability to produce extracellular, cold-active, alkaline, and detergent-stable protease was isolated from soil samples obtained from Gangotri glacier, Western Himalaya, India. The culture conditions for higher...

  • Eco-friendly preparatory process for silk: Degumming by protease enzyme. Gowda, K. N. Ninge; Padaki, Naveen V.; Sudhakar, R.; Subramani, R. // Man-Made Textiles in India;Jan2007, Vol. 50 Issue 1, p28 

    Increased awareness and concerns about the environment and pollution have paved way for Eco-friendly processes in chemical processing. Conventional soap- soda boiling method of degumming silk has many disadvantages coupled with the convenience of time. The enzymatic degumming processes have been...

  • Effects of Neutral Salts and Alcohols on the Activity of Streptomyces caespitosus Neutral Protease. Inouye, Kuniyo; Shimada, Takashi; Yasukawa, Kiyoshi // Journal of Biochemistry;Sep2007, Vol. 142 Issue 3, p317 

    Streptomyces caespitosus neutral protease (ScNP) is one of the smallest metalloproteinase with a molecular mass of 14 kDa. Effects of solvent composition on ScNP activity were examined using a peptide substrate. The kcat/Km values of ScNP exhibited bell-shaped pH-dependence with the optimal pH...

  • PROTEASE ACTIVITY OF PEPTOCOCCUS ACTIVUS. Shahina, Zinnat; Hossain, Mohammad Towhid; Hakim, Mohammad Abdul // International Journal of Current Research & Review;Aug2012, Vol. 4 Issue 16, p146 

    Peptococcus activus are anaerobic, non motile, non spore forming gram positive cocci. The objective of this study was to investigate the availability of this bacteria and their ability to protease production. Eleven different bacterial colonies were isolated from shrimp and dry fish(shrimp).Of...

  • Genetic Control of Extracellular Protease Synthesis in the Yeast Yarrowia lipolytica. Gonzalez-Lopez, Claudia I.; Szabo, Roman; Blanchin-Roland, Sylvie; Gaillardin, Claude // Genetics;Feb2002, Vol. 160 Issue 2, p417 

    Assesses the genetic control of extracellular protease synthesis in yeast. Evaluation on the hydrogen ion concentration (pH) for the growth medium of yeast; Response of alkaline protease to pH; Identification of homologs for Yarrowia lipolytica.

  • Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor are influenced by pH. Sidera, Christina; Chibuu Liu; Austen, Brian // BMC Biochemistry;2002, Vol. 3, p25 

    Background: One of the signatures of Alzheimer's disease is the accumulation of aggregated amyloid protein, Aβ, in the brain. Aβ arises from cleavage of the Amyloid Precursor protein by β and γ secretases, which present attractive candidates for therapeutic targeting. Two...

  • Effect of the Ph in the Conformation and Activity of the Acid Protease From Aspergillus saitoi. Tello-Solis, Salvador R. // Protein & Peptide Letters;Apr2001, Vol. 8 Issue 2, p101 

    The circular dichroism spectrum in the far UV-region (190-240 nm) indicates that the acid protease from Aspergillus saitoi contains appreciable amounts of beta-sheet. The structure-activity relationship of the protein is studied as a function of the pH.

  • Self-Assembling Systems Based on Amphiphilic Poly-N-vinylpyrrolidone and Their Interaction with Model Proteins. Villemson, A. L.; Malykh, E. V.; Shtilman, M. I.; Larionova, N. I. // Biochemistry (00062979);Aug2003, Vol. 68 Issue 8, p869 

    Polymeric particles formed by stearoyl-poly-N-vinylpyrrolidone (PVP-stear) of Mn = 2600 were obtained in aqueous solution, and their shape and size distribution were characterized. The size of the particles was shown to decrease with an increase in the ionic strength of the solution. Interaction...

  • Optimization of extracellular thermotolerant alkaline protease produced by marine Roseobacter sp. (MMD040). S. Shanmughapriya; J. Krishnaveni; Joseph Selvin; R. Gandhimathi; M. Arunkumar; T. Thangavelu; G. Kiran; K. Natarajaseenivasan // Bioprocess & Biosystems Engineering;Aug2008, Vol. 31 Issue 5, p427 

    Abstract  Marine endosymbiontic Roseobacter sp. (MMD040), which produced high yields of protease, was isolated from marine sponge Fasciospongia cavernosa, collected from the peninsular coast of India. Maximum production of enzyme was obtained in Luria-Bertani broth. Catabolite repression...

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics