02473nas a2200241   4500008004100000022001400041245013400055210006900189260007400258300001200332490000600344520154200350653002001892653002501912653002301937653002601960653001501986100002502001700002802026700002802054700002102082856012802103       2013                        eng d  a1872-885500aCompensatory proteolytic responses to dietary proteinase inhibitors from Albizia lebbeck seeds in the helicoverpa armigera larvae0 aCompensatory proteolytic responses to dietary proteinase inhibit  aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJUN  a259-2660 v73 a<p>Plant proteinase inhibitors (PIs) have been shown to reduce the growth rates in larvae of numerous insect species. On the other hand, insects can also regulate their proteinases against plant PIs. In the present study, we report the compensatory activities of Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) gut proteinases against the PIs of Albizia lebbeck seeds. Total of ten proteinase inhibitor bands were detected in the seed extract of A. lebbeck. Bioassays were conducted by feeding H. armigera larvae on diet containing partially purified PIs from A. lebbeck seeds. Results show that larval growth and survival was significantly reduced by A. lebbeck PIs. We found that higher activity H. armigera gut proteinase (HGP) isoforms observed in the midgut of control larvae were inhibited in the midgut of larvae fed on test diet. Some HGP isoforms were induced in the larvae fed on PI containing test diet; however, these isoforms showed lower activity in the larvae fed on control diet. Aminopeptidase activities were significantly increased in the midgut of larvae fed on test diet. A population of susceptible and resistant enzymes was observed in the midgut of H. armigera, when fed on diet containing PIs from A. lebbeck seeds. Our initial observations indicate that H. armigera can regulate its digestive proteinase activity against non-host plant PIs, too. It is important to study the exact biochemical and molecular mechanisms underlying this phenomenon in order to develop PI-based insect control strategies.</p>10aAlbizia lebbeck10aHelicoverpa armigera10aMidgut proteinases10aProteinase inhibitors10aregulation1 aHivrale, Vandana, K.1 aLomate, Purushottam, R.1 aBasaiyye, Shriniwas, S.1 aKalve, Neeta, D.  uhttps://library.ncl.res.in/content/compensatory-proteolytic-responses-dietary-proteinase-inhibitors-albizia-lebbeck-seeds-002266nas a2200277   4500008004100000022001400041245007800055210006900133260009200202300001200294490000700306520130400313653001601617653002001633653001701653653001901670653001801689653001901707653001501726653001501741100002901756700002801785700002601813700003501839856011401874       2016                        eng d  a0738-855100aPenicillin acylases revisited: importance beyond their industrial utility0 aPenicillin acylases revisited importance beyond their industrial  a4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLANDbTAYLOR & FRANCIS LTDcMAR  a303-3160 v363 a<p>It is of great importance to study the physiological roles of enzymes in nature; however, in some cases, it is not easily apparent. Penicillin acylases are pharmaceutically important enzymes that cleave the acyl side chains of penicillins, thus paving the way for production of newer semi-synthetic antibiotics. They are classified according to the type of penicillin (G or V) that they preferentially hydrolyze. Penicillin acylases are also used in the resolution of racemic mixtures and peptide synthesis. However, it is rather unfortunate that the focus on the use of penicillin acylases for industrial applications has stolen the spotlight from the study of the importance of these enzymes in natural metabolism. The penicillin acylases, so far characterized from different organisms, show differences in their structural nature and substrate spectrum. These enzymes are also closely related to the bacterial signalling phenomenon, quorum sensing, as detailed in this review. This review details studies on biochemical and structural characteristics of recently discovered penicillin acylases. We also attempt to organize the available insights into the possible in vivo role of penicillin acylases and related enzymes and emphasize the need to refocus research efforts in this direction.</p>10abeta-lactam10acholoyl glycine10ain vivo role10aNtn hydrolases10apathogenicity10aquorum sensing10aregulation10asignalling1 aAvinash, Vellore, Sunder1 aPundle, Archana, Vishnu1 aRamasamy, Sureshkumar1 aSuresh, Cheravakkattu, Gopalan  uhttps://library.ncl.res.in/content/penicillin-acylases-revisited-importance-beyond-their-industrial-utility-002489nas a2200265   4500008004100000022001400041245019300055210006900248260000800317300001000325490000700335520152800342653001401870653001201884653001601896653001501912653001401927653001401941100002301955700002701978700003102005700003102036700002602067856013002093       2023                        eng d  a1939-123400aCellulase hyper-producing fungus penicillium janthinellum NCIM 1366 elaborates a wider array of proteins involved in transport and secretion, potentially enabling a diverse substrate range0 aCellulase hyperproducing fungus penicillium janthinellum NCIM 13  cMAR  a61-730 v163 a<p>
	The efficient breakdown of lignocellulose requires the concerted activity of multiple enzymes. Previous studies on Penicillium janthinellum NCIM 1366 (PJ-1366) have revealed a more versatile repertoire of cellulases as compared to the hypercellulolytic strain Trichoderma reesei RUT-C30. Since a robust transport and secretion network is necessary to achieve proficient enzyme production, the transporters and extracellular proteins of PJ-1366 identified from its genome data were compared with those of Penicillium rolfsii (the phylogenetically closest species) and T. reesei RUT-C30 (the industrial work horse for cellulase production). Transmembrane proteins formed 20.4%, 21.0% and 18.2%, respectively of the proteome of PJ-1366, P. rolfsii and T. reesei RUT-C30, and 292 of them were mapped as transporters in PJ-1366. Major facilitator superfamily transporters (264) and sugar transporters (167) are abundant in PJ-1366, which probably aid in the uptake of oligosaccharide inducers of cellulase. The number of extracellular proteins (1007) in PJ-1366 is the highest reported for a Penicillium species. Also, PJ-1366 encoded 1.5 x more proteins involved in carbohydrate metabolism than the other fungi, and its secreted CAZymes belonged to much more diverse families (73), potentially enabling the fungus to act on heterogenous substrates. Structural differences in some untranslated protein response (UPR) effectors like Pdi and Clx detected in PJ-1366 may facilitate unique modes of cellulase regulation.</p>
10aCellulase10aPathway10aPenicillium10aregulation10aSecretion10aTransport1 aChristopher, Meera1 aSreeja-Raju, Athiraraj1 aKooloth-Valappil, Prajeesh1 aGokhale, Digambar, Vitthal1 aSukumaran, Rajeev, K.  uhttps://library.ncl.res.in/content/cellulase-hyper-producing-fungus-penicillium-janthinellum-ncim-1366-elaborates-wider-array