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-002914nas a2200337   4500008004100000022001400041245014400055210006900199260009200268300001200360490000700372520169100379653002702070653002302097653001402120653002502134653002702159653001102186653002702197653001302224100002302237700002802260700002202288700002402310700002102334700002402355700002102379700002002400700002602420856013002446       2008                        eng d  a0958-315700aEffect of repeated in vitro sub-culturing on the virulence of metarhizium anisopliae against helicoverpa armigera (Lepidoptera : Noctuidae)0 aEffect of repeated in vitro subculturing on the virulence of met  a4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLANDbTAYLOR & FRANCIS LTDcMAY  a337-3550 v183 a<p>The effect of repeated conidial sub-culturing of Metarhizium anisopliae on its virulence against Helicoverpa armigera (Hbner) was studied. The LT(50) observed against third instar larvae of H. armigera for the first sub-culture was 3.4 days; it increased to 4.5 and 5.6 days for the 20th and the 40th sub-cultures, respectively. The LT50 values after passage of the 40th sub-culture on H. armigera decreased to 4.4 and 3.7 days for the 40th (first in vivo) and the 40th (fifth in vivo) passages, respectively. Similarly, the LC(50) of M. anisopliae towards third instar larvae of H. armigera increased from the first sub-culture (0.17x10(4)) to (3.0x10(4)) for the 40th conidial transfers on potato dextrose agar and again decreased to 0.74x10(4) and 0.23x10(4) in the 40th (first in vivo) and the 40th (fifth in vivo) passage, respectively. Similar trends for LC(50) and LT(50) values were seen when sugarcane woolly aphid, Ceratovacuna lanigera Zehntner was used as a host. Significant variation in appressorium formation and cuticle-degrading enzyme production such as chitinase, chitin deacetylase, chitosanase and protease during subsequent sub-culturing and passage through H. armigera was observed. Though there was no effect on internal transcribed spacer (ITS) sequence pattern, interestingly, in randomly amplified polymorphic DNA (RAPD), significant differences in the band intensities and in the banding pattern for different sub-cultures of M. anisopliae were observed. As stable virulence towards the insect pest is desirable for commercialisation of a mycoinsecticide, such changes in virulence due to repeated in vitro transfer need to be monitored and minimised.</p>10aappressorium formation10achitin deacetylase10achitinase10aHelicoverpa armigera10ain vitro sub-culturing10aLipase10aMetarhizium anisopliae10aProtease1 aNahar, Pallavi, B.1 aKulkarni, Shuklangi, A.1 aKulye, Mahesh, S.1 aChavan, Santosh, B.1 aKulkarni, Girish1 aRajendran, Armugham1 aYadav, Priya, D.1 aShouche, Yogesh1 aDeshpande, Mukund, V.  uhttps://library.ncl.res.in/content/effect-repeated-vitro-sub-culturing-virulence-metarhizium-anisopliae-against-helicoverpa-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