02410nas a2200337   4500008004100000022001400041245011600055210006900171260009200240300001200332490000700344520123200351653002701583653002301610653001401633653001601647653002501663653001101688653002701699653001301726100002801739700002201767700002101789700002001810700002401830700002301854700002201877700002001899700002601919856012701945       2008                        eng d  a0958-315700aComparison of Metarhizium isolates for biocontrol of helicoverpa armigera (Lepidoptera : Noctuidae) in chickpea0 aComparison of Metarhizium isolates for biocontrol of helicoverpa  a4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLANDbTAYLOR & FRANCIS LTDcFEB  a809-8280 v183 a<p>Metarhizium isolates from soil (53) and insect hosts (10) were evaluated for extracellular production of cuticle degrading enzyme (CDE) activities such as chitinase, chitin deacetylase (CDA), chitosanase, protease and lipase. Regression analysis demonstrated the relation of CDE activities with Helicoverpa armigera mortality. On basis of this relation, ten isolates were selected for further evaluation. Subsequently, based on LT(50) of the 10 isolates towards H. armigera, five isolates were selected. Out of these five isolates, three were selected on the basis of higher conidia production (60-75 g/kg rice), faster sedimentation time (ST(50)) (2.3-2.65 h in 0.1% (w/v) Tween 80) and lower LC(50) (1.4- 5.7 x 10(3) conidia/mL) against H. armigera. Finally, three Metarhizium isolates were selected for the molecular fingerprinting using ITS sequencing and RAPD patterning. All three isolates, M34412, M34311 and M81123, showed comparable RAPD patterns with a 935G primer. These were further evaluated for their field performance against H. armigera in a chickpea crop. The percent efficacies with the three Metarhizium isolates were from 65 to 72%, which was comparable to the chemical insecticide, endosulfan (74%).</p>10aappressorium formation10achitin deacetylase10achitinase10achitosanase10aHelicoverpa armigera10aLipase10aMetarhizium anisopliae10aProtease1 aKulkarni, Shuklangi, A.1 aGhormade, Vandana1 aKulkarni, Girish1 aKapoor, Manisha1 aChavan, Santosh, B.1 aRajendran, Armugam1 aPatil, Sanjay, K.1 aShouche, Yogesh1 aDeshpande, Mukund, V.  uhttps://library.ncl.res.in/content/comparison-metarhizium-isolates-biocontrol-helicoverpa-armigera-lepidoptera-noctuidae-002014nas a2200217   4500008004100000022001400041245007600055210006900131260006700200300001200267490000700279520124500286653002301531653001401554653001601568653003301584653003301617100001901650700002601669856010101695       2013                        eng d  a8756-793800aChitinolytic enzymes: an appraisal as a product of commercial potential0 aChitinolytic enzymes an appraisal as a product of commercial pot  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJUL  a833-8460 v293 a<p>Chitin, its deacetylated form, chitosan and chitinolytic enzymes viz. endo-chitinase, N-acetylglucosaminidase, chitosanase, chitin deacetylase (CDA) are gaining importance for their biotechnological applications. Presently, chitin degrading enzymes constitute high-cost low-volume products in human health care and associated research. Indeed chitinases and CDA-chitosanase complex possesss tremendous potential in agriculture to control plant pathogenic fungi and insects. The success in exploring chitinases especially for agriculture, i.e. as a high-volume low-cost product, depends on the availability of highly active preparations with a reasonable cost. Therefore, a reconsideration in terms of understanding the roles of chitinolytic enzymes in applications, e.g. host-pathogen interaction for biocontrol, different mechanisms of chitin degradation, and identification of new enzymes with varying specificities, may make them more useful in a variety of commercial processes in the near future. The possible issues and challenges encountered in the translation of proof of concept into a commercial product will be appraised in this review. (c) 2013 American Institute of Chemical Engineers Biotechnol. Prog., 29:833-846, 2013</p>10achitin deacetylase10achitinase10achitosanase10ahigh-cost low-volume product10ahigh-volume low-cost product1 aChavan, S., B.1 aDeshpande, Mukund, V.  uhttps://library.ncl.res.in/content/chitinolytic-enzymes-appraisal-product-commercial-potential-0