@article { ISI:000319229900002,
	title = {Compensatory proteolytic responses to dietary proteinase inhibitors from Albizia lebbeck seeds in the helicoverpa armigera larvae},
	journal = {Arthropod-Plant Interactions},
	volume = {7},
	number = {3},
	year = {2013},
	month = {JUN},
	pages = {259-266},
	publisher = {SPRINGER},
	address = {VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS},
	abstract = {<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>},
	keywords = {Albizia lebbeck, Helicoverpa armigera, Midgut proteinases, Proteinase inhibitors, regulation},
	issn = {1872-8855},
	doi = {10.1007/s11829-012-9240-1},
	author = {Hivrale, Vandana K. and Lomate, Purushottam R. and Basaiyye, Shriniwas S. and Kalve, Neeta D.}
}
@article { ISI:000367612000010,
	title = {Penicillin acylases revisited: importance beyond their industrial utility},
	journal = {Critical Reviews In Biotechnology},
	volume = {36},
	number = {2},
	year = {2016},
	month = {MAR},
	pages = {303-316},
	publisher = {TAYLOR \& FRANCIS LTD},
	address = {4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLAND},
	abstract = {<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>},
	keywords = {beta-lactam, choloyl glycine, in vivo role, Ntn hydrolases, pathogenicity, quorum sensing, regulation, signalling},
	issn = {0738-8551},
	doi = {10.3109/07388551.2014.960359},
	author = {Avinash, Vellore Sunder and Pundle, Archana Vishnu and Ramasamy, Sureshkumar and Suresh, Cheravakkattu Gopalan}
}
