@article { ISI:000257228100019,
	title = {Optimal xylanase production using Penicilium janthinellum NCIM 1169: a model based approach},
	journal = {Biochemical Engineering Journal},
	volume = {40},
	number = {2},
	year = {2008},
	month = {JUN},
	pages = {348-356},
	publisher = {ELSEVIER SCIENCE SA},
	address = {PO BOX 564, 1001 LAUSANNE, SWITZERLAND},
	abstract = {<p>Xylanases are an industrially important class of hydrolytic enzymes that degrade xylans. Production of xylanase from a fungal culture by submerged fermentation and optimization of the operating conditions for maximum activity are the two aims of the present study. Penicillium janthinellum NCIM 1169 with Mandels-Weber medium, sugarcane bagassse (40\#) as a carbon source and beef extract as a nitrogen source were used in the experiments. We did 41 experiments to see the effect of variations in carbon, nitrogen source, pH, and inoculum on xylanase activity. This data was then used to build an input/output model using multiple linear regression, back propagation neural network and lazy learning algorithm. It was found that lazy learning model correlated well in mapping input/output data. This model was then utilized as an objective function in genetic algorithm to find the optimal combination of the operating conditions to get the maximum xylanase activity. It was observed that with carbon source, 1.63\%, nitrogen source, 0.16\%, pH, 4.1, and inoculum, 5.5\%, maximum xylanase activity of 28.98 +/- 1.73 U/ml was achieved. (C) 2008 Elsevier B.V. All rights reserved.</p>},
	keywords = {Artificial intelligence, Enzyme activity, Fermentation, Modeling, Optimization, Xylanase},
	issn = {1369-703X},
	doi = {10.1016/j.bej.2008.01.003},
	author = {Meshram, Mukesh and Kulkarni, Abhijit and Jayaraman, Valadi K. and Kulkarni, B. D. and Lele, S. S.}
}
@article { ISI:000359173900007,
	title = {Biochemical, structural and functional diversity between two digestive alpha-amylases from helicoverpa armigera},
	journal = {Biochimica Et Biophysica Acta-General Subjects},
	volume = {1850},
	number = {9},
	year = {2015},
	month = {SEP},
	pages = {1719-1728},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Background: Helicoverpa armigera (Lepidoptera) feeds on various plants using diverse digestive enzymes as one of the survival tool-kit. The aim of the present study was to understand biochemical properties of recombinant alpha-amylases of H. armigera viz., HaAmy1 and HaAmy2. Methods: The open reading frames of HaAmy1 and HaAmy2 were cloned in Pichia pastoris and expressed heterologously. Purified recombinant enzymes were characterized for their biochemical and biophysical attributes using established methods. Results: Sequence alignment and homology modeling showed that HaAmy1 and HaAmy2 were conserved in their amino acid sequences and structures. HaAmy1 and HaAmy2 showed optimum activity at 60 degrees C; however, they differed in their optimum pH. Furthermore, HaAmy2 showed higher affinity for starch and amylopectin whereas HaAmy1 had higher catalytic efficiency. HaAmy1 and HaAmy2 were inhibited to the same magnitude by a synthetic amylase inhibitor (acarbose) while wheat amylase inhibitor showed about 2-fold higher inhibition of HaAmy1 than HaAmy2 at pH 7 while 6-fold difference at pH 11. Interactions of HaAmy1 and HaAmy2 with wheat amylase inhibitor revealed 2:1 stoichiometric ratio and much more complex interaction with HaAmy1. Conclusions: The diversity of amylases in perspective of their biochemical and biophysical properties, and their differential interactions with amylase inhibitors signify the potential role of these enzymes in adaptation of H. armigera on diverse plant diets. General significance: Characterization of digestive enzymes of H. armigera provides the molecular basis for the polyphagous nature and thus could assist in designing future strategies for the insect control. (C) 2015 Elsevier B.V. All rights reserved.</p>},
	keywords = {alpha-amylases, Amylase inhibitors, Digestive enzymes, Enzyme activity, Helicoverpa armigera},
	issn = {0304-4165},
	doi = {10.1016/j.bbagen.2015.04.008},
	author = {Bhide, Amey J. and Channale, Sonal M. and Patil, Sucheta S. and Gupta, Vidya S. and Ramasamy, Sureshkumar and Giri, Ashok P.}
}
