@article { ISI:000368189500001,
	title = {Potential dual role of eugenol in inhibiting advanced glycation end products in diabetes: proteomic and mechanistic insights},
	journal = {Scientific Reports},
	volume = {6},
	year = {2016},
	month = {JAN},
	publisher = {NATURE PUBLISHING GROUP},
	address = {MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND},
	abstract = {<p>Medicinally important genus Ocimum harbors a vast pool of chemically diverse metabolites. Current study aims at identifying anti-diabetic candidate compounds from Ocimum species. Major metabolites in O. kilimandscharicum, O. tenuiflorum, O. gratissimum were purified, characterized and evaluated for anti-glycation activity. In vitro inhibition of advanced glycation end products (AGEs) by eugenol was found to be highest. Preliminary biophysical analysis and blind docking studies to understand eugenol-albumin interaction indicated eugenol to possess strong binding affinity for surface exposed lysines. However, binding of eugenol to bovine serum albumin (BSA) did not result in significant change in secondary structure of protein. In vivo diabetic mice model studies with eugenol showed reduction in blood glucose levels by 38\% likely due to inhibition of alpha-glucosidase while insulin and glycated hemoglobin levels remain unchanged. Western blotting using anti-AGE antibody and mass spectrometry detected notably fewer AGE modified peptides upon eugenol treatment both in vivo and in vitro. Histopathological examination revealed comparatively lesser lesions in eugenol-treated mice. Thus, we propose eugenol has dual mode of action in combating diabetes; it lowers blood glucose by inhibiting a-glucosidase and prevents AGE formation by binding to epsilon-amine group on lysine, protecting it from glycation, offering potential use in diabetic management.</p>},
	issn = {2045-2322},
	doi = {10.1038/srep18798},
	author = {Singh, Priyanka and Jayaramaiah, Ramesha H. and Agawane, Sachin B. and Vannuruswamy, Garikapati and Korwar, Arvind M. and Anand, Atul and Dhaygude, Vitthal S. and Shaikh, Mahemud L. and Joshi, Rakesh S. and Boppana, Ramanamurthy and Kulkarni, Mahesh J. and Thulasiram, Hirekodathakallu V. and Giri, Ashok P.}
}
@article {47778,
	title = {Performance of Aspergillus niger (NCIM 563) phytase based feed supplement for broiler growth and phosphorus excretion},
	journal = {Biocatalysis and Agricultural Biotechnology},
	volume = {31},
	year = {2021},
	month = {JAN},
	pages = {101887},
	type = {Article},
	abstract = {Despite availability of commercial enzymes, the phytase produced from relatively inexpensive systems with high yields are gaining global attention in the feed industries in post-antibiotic era. We studied A. niger NCIM 563 Phytase produced in solid state fermentation (SSF) derived Koji powder and evaluated its utility in the poultry feed for broiler growth performance and phosphorous (P) excretion. The ability of phytase in the dried powder was estimated to dephytinize the poultry feed under simulated gastric conditions. Poultry feed was formulated using A. niger NCIM 563 phytase followed by a 42 days feed trial on broilers. After supplementation of phytase to the diet, there was a reduction of dietary P, maintained growth performance, skeletal development of broilers and reduced levels of phytic acid and available P in the litter. Extracellular phytase was able to replace up to 0.1\% P in poultry feed. Minimal downstream processing a low-cost feed supplement with significant phytase activity could provide added advantage for anti-nutrition free poultry feed.},
	keywords = {Phosphorus, Phytase, Poultry feed, Solid state fermentation},
	isbn = {1878-8181},
	doi = {10.1016/j.bcab.2020.101887},
	url = {https://www.sciencedirect.com/science/article/pii/S1878818120319186},
	author = {Puppala, Kumar Raja and Buddhiwant, Priyanka G. and Agawane, Sachin B. and Kadam, Avinash S. and Mote, Chandrashekhar S. and Lonkar, Vijaysinh D. and Khire, Jayant M. and Dharne, Mahesh S.}
}
