Induction of leucine aminopeptidase (LAP) like activity with wounding and methyl jasmonate in pigeonpea (Cajanas cajan) suggests the role of these enzymes in plant defense in leguminosae

Lomate, Purushottam R.; Hivrale, Vandana K.

doi:10.1016/j.plaphy.2011.02.023

Cited by 13 publications

(9 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The stability of the fibrinolytic enzyme with respect to temperature was estimated by incubating it in the absence of substrate at different temperatures, 30–70 °C for 1 h. Fibrinolytic activity of the enzyme was assayed as described earlier. To elucidate the influence of divalent ions on enzyme activity, the enzyme was incubated for 30 min along with different divalent ions, namely Ca 2+ , Cu 2+ , Co 2+ , Mg 2+ , Mn 2+ , Hg 2+ , Fe 2+ , and Zn 2+ at 0.01 M concentrations (Lomate and Hivrale 2011). …”

Section: Methodsmentioning

confidence: 99%

Bio-prospecting of cuttle fish waste and cow dung for the production of fibrinolytic enzyme from Bacillus cereus IND5 in solid state fermentation

Devadhasan¹,

Arumugaperumal

Muthulakshmi

et al. 2016

3 Biotech

View full text Add to dashboard Cite

The process parameters governing the production of fibrinolytic enzyme in solid state fermentation employing Bacillus cereus IND5 and using cuttle fish waste and cow dung substrate were optimized. The pH value of the medium, moisture content, sucrose, casein and magnesium sulfate were considered for two-level full factorial design and pH, casein and magnesium sulfate were identified as the important factors for fibrinolytic enzyme production. Central composite design was applied to investigate the interactive effect among variables (pH, casein and magnesium sulfate) and response surface plots were created to find the pinnacle of process response. The optimized levels of factors were pH 7.8, 1.1% casein and 0.1% magnesium sulfate. Enzyme production was increased 2.5-fold after statistical approach. The enzyme was purified up to a specific activity of 364.5 U/g proteins and its molecular weight was 47 kDa. It was stable at pH 8.0 and was highly active at 50 °C. The mixture of cuttle fish waste and cow dung could find great application as solid substrate for the production of fibrinolytic enzyme.

show abstract

Section: Methodsmentioning

confidence: 99%

Bio-prospecting of cuttle fish waste and cow dung for the production of fibrinolytic enzyme from Bacillus cereus IND5 in solid state fermentation

Devadhasan¹,

Arumugaperumal

Muthulakshmi

et al. 2016

3 Biotech

View full text Add to dashboard Cite

show abstract

“…In the present paper we have tried to explore the same. Earlier we have characterized jasmonate inducible aminopeptidase from pigeon pea [18] and soluble aminopeptidases from the midgut of H. armigera [19]. Here, we report the effects of pigeon pea inducible aminopeptidase in the midgut of H. armigera .…”

Section: Introductionmentioning

confidence: 82%

“…It was reported that LAP-A has a role in modulating defenses against herbivores by promoting late wound responses and acting downstream of JA biosynthesis and perception [17]. Earlier, we have been reported the induction of LAP-like enzyme in non-solanaceous plant namely pigeon pea ( Cajanas cajan ) after wounding and application of MeJA [18]. LAP-A was among the most abundant jasmonate inducible proteins identified in the midgut of M. sexta larvae grown on induced plants [9].…”

Section: Introductionmentioning

confidence: 86%

“…The purified inducible aminopeptidase was used for insect feeding assays. First step of LAP purification was performed as described earlier [18] and further using additional two steps of gel filtration and one step of ion-exchange chromatography. Aminopeptidase activity fractions obtained from gel filtration chromatography were concentrated with acetone precipitation and loaded on DEAE-cellulose anion-exchange column (2.5×23 cm) equilibrated with 0.1 M Tris–HCl pH 8.0.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Alterations in the Helicoverpa armigera Midgut Digestive Physiology after Ingestion of Pigeon Pea Inducible Leucine Aminopeptidase

et al. 2013

Self Cite

View full text Add to dashboard Cite

Jasmonate inducible plant leucine aminopeptidase (LAP) is proposed to serve as direct defense in the insect midgut. However, exact functions of inducible plant LAPs in the insect midgut remain to be estimated. In the present investigation, we report the direct defensive role of pigeon pea inducible LAP in the midgut of Helicoverpa armigera (Lepidoptera: Noctuidae) and responses of midgut soluble aminopeptidases and serine proteinases upon LAP ingestion. Larval growth and survival was significantly reduced on the diets supplemented with pigeon pea LAP. Aminopeptidase activities in larvae remain unaltered in presence or absence of inducible LAP in the diet. On the contrary, serine proteinase activities were significantly decreased in the larvae reared on pigeon pea LAP containing diet as compared to larvae fed on diet without LAP. Our data suggest that pigeon pea inducible LAP is responsible for the degradation of midgut serine proteinases upon ingestion. Reduction in the aminopeptidase activity with LpNA in the H. armigera larvae was compensated with an induction of aminopeptidase activity with ApNA. Our findings could be helpful to further dissect the roles of plant inducible LAPs in the direct plant defense against herbivory.

show abstract

“…[34] Subsequently, five models were generated and assessed on the basis of RMSD and TM-score. This online server theoretically measures various physicochemical parameters such as molecular mass.…”

Section: Methodsmentioning

confidence: 99%

Structural and biophysical characterization of cajanus cajan protease inhibitor

et al. 2017

View full text Add to dashboard Cite

Context:A large number of studies have proven that Protease inhibitors (PIs), specifically serine protease inhibitors, show immense divergence in regulation of proteolysis by targeting their specific proteases and hence, they play a key role in healthcare.Objective:We aimed to access in-vitro anticancer potential of PI from Cajanus cajan (CCPI). Also, crystallization of CCPI was targetted alongwith structure determination and its structure-function relationship.Materials and Methods:CCPI was purified from Cajanus cajan seeds by chromatographic techniques. The purity and molecular mass was determined by SDS-PAGE. Anticancer potential of CCPI was determined by MTT assay in normal HEK and cancerous A549 cells. The crystallization screening of CCPI was performed by commercially available screens. CCPI sequence was subject to BLASTp with homologous PIs. Progressive multiple alignment was performed using clustalw2 and was modelled using ab initio protocol of I-TASSER.Results:The results showed ~14kDa CCPI was purified in homogeneity. Also, CCPI showed low cytotoxic effects of in HEK i.e., 27% as compared with 51% cytotoxicity in A549 cells. CCPI crystallized at 16°C using 15% PEG 6000 in 0.1M potassium phosphate buffer (pH 6.0) in 2-3weeks as rod or needles visualized as clusters under the microscope. The molecular modelling revealed that it contains 3 beta sheets, 3 beta hairpins, 2 β-bulges, 6 strands, 3 helices, 1helix-helix interaction, 41 β-turns and 27 γ-turns.Discussion and Conclusion:The results indicate that CCPI may help to treat cancer in vivo aswell. Also, this is the first report on preliminary crystallization and structural studies of CCPI.

show abstract

Induction of leucine aminopeptidase (LAP) like activity with wounding and methyl jasmonate in pigeonpea (Cajanas cajan) suggests the role of these enzymes in plant defense in leguminosae

Cited by 13 publications

References 37 publications

Bio-prospecting of cuttle fish waste and cow dung for the production of fibrinolytic enzyme from Bacillus cereus IND5 in solid state fermentation

Bio-prospecting of cuttle fish waste and cow dung for the production of fibrinolytic enzyme from Bacillus cereus IND5 in solid state fermentation

Alterations in the Helicoverpa armigera Midgut Digestive Physiology after Ingestion of Pigeon Pea Inducible Leucine Aminopeptidase

Structural and biophysical characterization of cajanus cajan protease inhibitor

Contact Info

Product

Resources

About