02105nas a2200253   4500008004100000022001400041245016500055210006900220260009900289300001400388490000800402520111200410653000901522653001801531653002901549653001301578653002001591100002101611700002401632700002101656700002401677700002201701856012801723       2012                        eng d  a0308-814600aDiscovering bisdemethoxycurcumin from curcuma longa rhizome as a potent small molecule inhibitor of human pancreatic alpha-amylase, a target for type-2 diabetes0 aDiscovering bisdemethoxycurcumin from curcuma longa rhizome as a  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcDEC  a2638-26420 v1353 a<p>Curcuma longa rhizome is used extensively in culinary preparations in Far East and South-East Asia. Health benefits of curcuminoids from C. longa as antioxidants, anti-cancer and anti-inflammatory molecules have been well documented. We report here for the first time that Bisdemethoxycurcumin (BDMC) from C. longa, acts as an inhibitor to inactivate human pancreatic alpha-amylase, a therapeutic target for oral hypoglycemic agents in type-2 diabetes. Bioactivity guided isolation of rhizome isopropanol extract led to the identification by HPLC and NMR of BDMC as a lead small molecule inhibitor of porcine and human pancreatic alpha-amylase with an IC50 value of 0.026 and 0.025 mM, respectively. Kinetic analysis revealed that using starch as the substrate, HPA exhibited an uncompetitive mode of inhibition with an apparent K-i of 3.0 mu M. The study gains importance as BDMC could be a good drug candidate in development of new inhibitors of HPA and of functional foods for controlling starch digestion in order to reduce post-prandial hyperglycemia. (C) 2012 Elsevier Ltd. All rights reserved.</p>10aBDMC10aCurcuma longa10aHuman pancreatic amylase10akinetics10aType-2 diabetes1 aPonnusamy, Sudha1 aZinjarde, Smita, S.1 aBhargava, Shobha1 aRajamohanan, P., R.1 aRaviKumar, Ameeta  uhttps://library.ncl.res.in/content/discovering-bisdemethoxycurcumin-curcuma-longa-rhizome-potent-small-molecule-inhibitor-002127nas a2200265   4500008004100000022001400041245012200055210006900177260009900246300001200345490000800357520114100365653002501506653001401531653003701545653002701582653000901609100001901618700001701637700002401654700002201678700001601700700002101716856012401737       2015                        eng d  a0960-852400aConversion of dried aspergillus candidus mycelia grown on waste whey to biodiesel by in situ acid transesterification0 aConversion of dried aspergillus candidus mycelia grown on waste   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcDEC  a502-5070 v1973 a<p>This study reports optimization of the transesterification reaction step on dried biomass of an oleaginous fungus Aspergillus candidus grown on agro-dairy waste, whey. Acid catalyzed transesterification was performed and variables affecting esterification, viz., catalyst methanol and chloroform concentrations, temperature, time, and biomass were investigated. Statistical optimization of the transesterification reaction using Plackett-Burman Design showed biomass to be the predominant factor with a 12.5-fold increase in total FAME from 25.6 to 320 mg. Studies indicate that the transesterification efficiency in terms of conversion is favored by employing lower biomass loadings. A. candidus exhibited FAME profiles containing desirable saturated (30.2%), monounsaturated (31.5%) and polyunsaturated methyl esters (38.3%). The predicted and experimentally determined biodiesel properties (density, kinematic viscosity, iodine value, cetane number, TAN, water content, total and free glycerol) were in accordance with international (ASTM D6751, EN 14214) and national (IS 15607) standards. (C) 2015 Published by Elsevier Ltd.</p>10aAspergillus candidus10aBiodiesel10aIn situ acid transesterification10aPlackett-Burman Design10aWhey1 aKakkad, Hardik1 aKhot, Mahesh1 aZinjarde, Smita, S.1 aRaviKumar, Ameeta1 aKumar, Ravi1 aKulkarni, B., D.  uhttps://library.ncl.res.in/content/conversion-dried-aspergillus-candidus-mycelia-grown-waste-whey-biodiesel-situ-acid-002652nas a2200205   4500008004100000022001400041245013700055210006900192260009100261300001300352490000700365520181000372100002102182700001902203700002202222700002402244700003302268700002202301856012302323       2015                        eng d  a1932-620300aGedunin and azadiradione: human pancreatic alpha-amylase inhibiting limonoids from neem (azadirachta indica) as anti-diabetic agents0 aGedunin and azadiradione human pancreatic alphaamylase inhibitin  a1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USAbPUBLIC LIBRARY SCIENCEcOCT  ae01401130 v103 a<p>Human pancreatic alpha-amylase (HPA) inhibitors offer an effective strategy to lower postprandial hyperglycemia via control of starch breakdown. Limonoids from Azadirachta indica known for their therapeutic potential were screened for pancreatic alpha-amylase inhibition, a known anti-diabetic target. Studies were carried out to reveal their mode of action so as to justify their hypoglycemic potential. Of the nine limonoids isolated/semi-synthesized from A. indica and screened for alpha-amylase inhibition, azadiradione and exhibited potential inhibition with an IC50 value of 74.17 and 68.38 mu M, respectively against HPA under in vitro conditions. Further screening on AR42J alpha-amylase secretory cell line for cytotoxicity and bioactivity revealed that azadiradione and gedunin exhibited cytotoxicity with IC50 of 11.1 and 13.4 mu M. Maximal secreted alpha-amylase inhibition of 41.8% and 53.4% was seen at 3.5 and 3.3 mu M, respectively. Michaelis-Menten kinetics suggested a mixed mode of inhibition with maltopentaose (K-i 42.2, 18.6 mu M) and starch (K-i' 75.8, 37.4 mu M) as substrate with a stiochiometry of 1: 1 for both azadiradione and gedunin, respectively. The molecular docking simulation indicated plausible p-alkyl and alkyl-alkyl interactions between the aromatic amino acids and inhibitors. Fluorescence and CD confirmed the involvement of tryptophan and tyrosine in ligand binding to HPA. Thermodynamic parameters suggested that binding is enthalpically and entropically driven with Delta G degrees of -21.25 kJ mol(-1) and -21.16 kJ mol(-1) for azadiradione and gedunin, respectively. Thus, the limonoids azadiradione and gedunin could bind and inactivate HPA (anti-diabetic target) and may prove to be lead drug candidates to reduce/control post-prandial hyperglycemia.</p>1 aPonnusamy, Sudha1 aHaldar, Saikat1 aMulani, Fayaj, A.1 aZinjarde, Smita, S.1 aThulasiram, Hirekodathakallu1 aRaviKumar, Ameeta  uhttps://library.ncl.res.in/content/gedunin-and-azadiradione-human-pancreatic-alpha-amylase-inhibiting-limonoids-neem-101628nas a2200193   4500008004100000245015300041210006900194260000800263300001200271490000700283520088500290100002201175700001901197700002401216700001601240700002601256700002201282856013001304       2016                        eng d00aRole of aliasing and interacting factors in the enhanced production of dehalogenase from Yarrowia lipolytica for degradation of brominated compounds0 aRole of aliasing and interacting factors in the enhanced product  cSEP  a114-1210 v413 aUse of persistent organobromines for industrial applications has led to their accumulation in environment. Yarrowia lipolytica NCIM 3589, a tropical marine yeast, degrades and detoxifies bromocompounds by an initial hydrolytic step. By optimizing culture conditions with 1-bromodecane as reference compound, the dehalogenase involved was remarkably enhanced 13-fold (384.13 U/ml) by a hybrid statistical Plackett-Burman and Box-Behnken design of experiments. Studies bring out in a novel way the role of aliasing and other masked interactions in growth media factors. Importantly, the enzyme acted on C3-C16 bromoalkanes and bromoaromatics, thereby generalizing the 'green chemistry' applicability of optimized media formulation for biotechnological applications. (C) 2016 The Korean Society of Industrial and Engineering Chemistry. Published by Elsevier B.V. All rights reserved.1 aVatsal, Aakanksha1 aPotdar, Chirag1 aZinjarde, Smita, S.1 aKumar, Ravi1 aKulkarni, Bhasker, D.1 aRaviKumar, Ameeta  uhttps://library.ncl.res.in/content/role-aliasing-and-interacting-factors-enhanced-production-dehalogenase-yarrowia-lipolytica