02695nas a2200301   4500008004100000022001400041245016000055210006900215260010600284300000900390490000700399520155800406653001301964653001801977653002801995653002902023653001502052653002402067100002402091700002002115700001902135700002002154700002202174700002302196700002602219700002002245856012802265       2016                        eng d  a0965-174800aCharacterization of two coleopteran alpha-amylases and molecular insights into their differential inhibition by synthetic alpha-amylase inhibitor, acarbose0 aCharacterization of two coleopteran alphaamylases and molecular   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcJUL  a1-110 v743 a<p>Post-harvest insect infestation of stored grains makes them unfit for human consumption and leads to severe economic loss. Here, we report functional and structural characterization of two coleopteran alpha-amylases viz. Callosobruchus chinensis alpha-amylase (CcAmy) and Tribolium castaneum alpha-amylase (TcAmy) along with their interactions with proteinaceous and non-proteinaceous alpha-amylase inhibitors. Secondary structural alignment of CcAmy and TcAmy with other coleopteran alpha-amylases revealed conserved motifs, active sites, di-sulfide bonds and two point mutations at spatially conserved substrate or inhibitor binding sites. Homology modeling and molecular docking showed structural differences between these two enzymes. Both the enzymes had similar optimum pH values but differed in their optimum temperature. Overall, pattern of enzyme stabilities were similar under various temperature and pH conditions. Further, CcAmy and TcAmy differed in their substrate affinity and catalytic efficiency towards starch and amylopectin. HPLC analysis detected common amylolytic products like maltose and maltotriose while glucose and malto-tetrose were unique in CcAmy and TcAmy catalyzed reactions respectively. At very low concentrations, wheat alpha-amylase inhibitor was found to be superior over the acarbose as far as complete inhibition of amylolytic activities of CcAmy and TcAmy was concerned. Mechanism underlying differential amylolytic reaction inhibition by acarbose was discussed. (C) 2016 Elsevier Ltd. All rights reserved.</p>10aAcarbose10aalpha-amylase10aalpha-amylase inhibitor10aCallosobruchus chinensis10aColeoptera10aTribolium castaneum1 aChannale, Sonal, M.1 aBhide, Amey, J.1 aYadav, Yashpal1 aKashyap, Garima1 aPawar, Pankaj, K.1 aMaheshwari, V., L.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P.  uhttp://library.ncl.res.in/content/characterization-two-coleopteran-alpha-amylases-and-molecular-insights-their-differential02628nas a2200229   4500008004100000245012800041210006900169260000800238300001200246490001000258520179900268100002002067700002402087700001902111700002602130700002202156700002302178700002102201700002602222700002002248856013002268       2017                        eng d00aGenomic and functional characterization of coleopteran insect-specific alpha-amylase inhibitor gene from amaranthus species0 aGenomic and functional characterization of coleopteran insectspe  cJUN  a319-3320 v 94  3 aThe smallest 32 amino acid alpha-amylase inhibitor from Amaranthus hypochondriacus (AAI) is reported. The complete gene of pre-protein (AhAI) encoding a 26 amino acid (aa) signal peptide followed by the 43 aa region and the previously identified 32 aa peptide was cloned successfully. Three cysteine residues and one disulfide bond conserved within known alpha-amylase inhibitors were present in AhAI. Identical genomic and open reading frame was found to be present in close relatives of A. hypochondriacus namely Amaranthus paniculatus, Achyranthes aspera and Celosia argentea. Interestingly, the 3'UTR of AhAI varied in these species. The highest expression of AhAI was observed in A. hypochondriacus inflorescence; however, it was not detected in the seed. We hypothesized that the inhibitor expressed in leaves and inflorescence might be transported to the seeds. Sub-cellular localization studies clearly indicated the involvement of AhAI signal peptide in extracellular secretion. Full length rAhAI showed differential inhibition against alpha-amylases from human, insects, fungi and bacteria. Particularly, alpha-amylases from Helicoverpa armigera (Lepidoptera) were not inhibited by AhAI while Tribolium castaneum and Callosobruchus chinensis (Coleoptera) alpha-amylases were completely inhibited. Molecular docking of AhAI revealed tighter interactions with active site residues of T. castaneum alpha-amylase compared to C. chinensis alpha-amylase, which could be the rationale behind the disparity in their IC50. Normal growth, development and adult emergence of C. chinensis were hampered after feeding on rAhAI. Altogether, the ability of AhAI to affect the growth of C. chinensis demonstrated its potential as an efficient bio-control agent, especially against stored grain pests.1 aBhide, Amey, J.1 aChannale, Sonal, M.1 aYadav, Yashpal1 aBhattacharjee, Kabita1 aPawar, Pankaj, K.1 aMaheshwari, V., L.1 aGupta, Vidya, S.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P.  uhttp://library.ncl.res.in/content/genomic-and-functional-characterization-coleopteran-insect-specific-alpha-amylase-inhibitor01931nas a2200241   4500008004100000022001400041245015700055210007000212260000800282300001200290490000700302520105000309653001501359653002801374653002301402653002001425653003301445100001801478700001701496700001801513700002301531856013501554       2019                        eng d  a1935-513000aProtein α-amylase inhibitor from withania somnifera and its role in overall quality and nutritional value improvement of potato chips during processing0 aProtein αamylase inhibitor from withania somnifera and its role   cAPR  a636-6440 v123 a<p>Cold storage and processing increase the reducing sugar level in potato (Solanum tuberosum L.) which is responsible for browning and acrylamide formation that adversely affect sensory and nutrient quality of chips. Effect of α-amylase inhibitor from Withania somnifera (WSAI) treatment on the overall quality improvement of potato chips during processing was studied. WSAI treatment to potato slices at 200 ppm for 30 min was found to reduce browning (60%), residual amylase, and polyphenol oxidase activities (~ 40%) and reduce sugar level by 25%, respectively, over control. Color match analysis indicated an improvement in whiteness and brightness indices and a significant reduction in yellowness index of potato chips. The treatment proved to be superior over blanching and reduction in acrylamide generation during frying was which also observed in chips treated with it. Furthermore, our results were comparable to that of treatment with α-amylase inhibitor of Triticum aestivum and better than synthetic inhibitor, acarbose.</p>
10aAcrylamide10aalpha-amylase inhibitor10aBrowning of potato10aReducing sugars10aSensory and nutrient quality1 aKasar, S., S.1 aGiri, A., P.1 aPawar, P., K.1 aMaheshwari, V., L.  uhttp://library.ncl.res.in/content/protein-%CE%B1-amylase-inhibitor-withania-somnifera-and-its-role-overall-quality-and-nutritional