@article { ISI:000272903900005,
	title = {Differential elicitation of an aspartic protease inhibitor: regulation of endogenous protease and initial events in germination in seeds of vigna radiata},
	journal = {Peptides},
	volume = {30},
	number = {12},
	year = {2009},
	month = {DEC},
	pages = {2118-2126},
	publisher = {ELSEVIER SCIENCE INC},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Plant aspartic proteases are of recent origin with their physiological significance in crucial processes emerging. Reports on the significance of aspartic protease inhibitors and their endogenous proteases in seeds of plants are scanty. This paper reports the purification of an aspartic protease inhibitor from the seeds of Vigna radiata, its control of the endogenous aspartic protease and their subsequent role in the early germination events. The role of the aspartic protease inhibitor and the enzyme in initial stages of germination of V. radiata has been tracked by differential timed expression and germination assays. The expression pattern revealed maximum expression of the inhibitor in the dormant seeds while the enzyme was predominant in the germinating seeds. Their expression patterns and interactions indicate their significance in initiation of germination. The expression of other classes of proteases was monitored during germination and a model predicting the events occurring during proteolysis of the storage protein in germination is hypothesized. The inhibitor was a linear, hydrophobic, pH stable and thermostable peptide with molecular weight of 1660 Da. The purified inhibitor showed a pI of 4.36 with the sequence as AEIYN KDGNK LDLYG. The inhibitor was found to be stable in a broad range of pH from 2 to 10 with an optimum of 3.0. The half-life of VrAPI at 100 degrees C was 30 min whereas the maximum activity was observed at 37 degrees C. The initial kinetic analysis of the inhibitor against the enclogenous protease showed an IC50 value of 11 nM while the value of the inhibition rate constant K-i was 34 x 10(-9) M. (C) 2009 Elsevier Inc. All rights reserved.</p>},
	keywords = {Aspartic protease, Plant proteases, Protease inhibitors, Vigna radiata},
	issn = {0196-9781},
	doi = {10.1016/j.peptides.2009.08.024},
	author = {Kulkarni, Aarohi and Rao, Mala}
}
@article { ISI:000310401100058,
	title = {Inhibition of xyloglucanase from an alkalothermophilic thermomonospora sp by a peptidic aspartic protease inhibitor from Penicillium sp VM24},
	journal = {Bioresource Technology},
	volume = {123},
	year = {2012},
	month = {NOV},
	pages = {390-399},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>A bifunctional inhibitor from Penicilliurn sp VM24 causing inactivation of xyloglucanase from Thermomonospora sp and an aspartic protease from Aspergillus saitoi was identified. Steady state kinetics studies of xyloglucanase and the inhibitor revealed an irreversible, non-competitive, two-step inhibition mechanism with IC50 and K-i; values of 780 and 500 nM respectively. The interaction of o-phthalaldehyde (OPTA)-labeled xyloglucanase with the inhibitor revealed that the inhibitor binds to the active site of the enzyme. Far- and near-UV spectrophotometric analysis suggests that the conformational changes induced in xyloglucanase by the inhibitor may be due to irreversible denaturation of enzyme. The bifunctional inhibitor may have potential as a biocontrol agent for the protection of plants against phytopathogenic fungi. (C) 2012 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Aspartic protease, Bifunctional inhibitor, Biocontrol agent, Inactivation mechanism, Xyloglucanase},
	issn = {0960-8524},
	doi = {10.1016/j.biortech.2012.07.050},
	author = {Menon, Vishnu and Rao, Mala}
}
