The seeds of the Yellow Bell Pepper (Capsicum annuum) were hand-collected from local farmers around La Plata, Buenos Aires, Argentina. The seeds were processed as previously described elsewhere [11 (link)]. The reagents sodium chloride, Coomassie Blue G-250, N,N,N′,N′-tetramethylethylenediamine (TEMED), tris (hydroxymethyl) aminomethane, sodium dodecyl sulphate (SDS), bovine serum albumin (BSA), β-mercaptoethanol (β ME), Nα-benzoyl-DL-arginine-p-nitroanilide (BApNA), and 4-nitrophenol-α-D-glucopyranoside (PNPG) were purchased from Sigma-Aldrich (San Luis, MO, USA). The proteases used in this study, such as Trypsin and α-Glucosidase, were obtained from Sigma-Aldrich. To perform PI purification, a Glyoxyl-agarose resin was obtained from FlukaTM. Fluconazole was purchased from Signa-Aldrich. All chemicals and reagents used in this study were of analytical grade, unless otherwise specified.
Nα benzoyl dl arginine p nitroanilide
Manufactured by Merck Group
Sourced in United States
Nα-benzoyl-DL-arginine-p-nitroanilide is a synthetic substrate used in biochemical assays to measure the activity of certain enzymes, particularly serine proteases. It is a colorimetric substrate that undergoes a visible color change upon enzymatic cleavage, allowing for the quantification of enzyme activity.
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Lab products found in correlation
Trypsin, by Merck Group (3 mentions)
Bovine serum albumin (bsa), by Merck Group (2 mentions)
Bis acrylamide, by Merck Group (2 mentions)
Acrylamide, by Merck Group (2 mentions)
N glutaryl l phenylalanine p nitroanilide, by Merck Group (2 mentions)
Sodium dodecyl sulfate (sds), by Merck Group (2 mentions)
4 nitrophenol α d glucopyranoside, by Merck Group (1 mentions)
Coomassie blue g 250, by Merck Group (1 mentions)
β mercaptoethanol, by Merck Group (1 mentions)
α glucosidase, by Merck Group (1 mentions)
Sephadex g 75, by Cytiva (1 mentions)
Soybean trypsin inhibitor, by Merck Group (1 mentions)
Temed, by Merck Group (1 mentions)
Tetramethylethylenediamine temed, by Merck Group (1 mentions)
Ammonium persulfate, by Merck Group (1 mentions)
Phenylmethylsulfonyl fluoride, by Merck Group (1 mentions)
Sodium phosphate, by Merck Group (1 mentions)
Furosemide, by Merck Group (1 mentions)
Tween 20, by Merck Group (1 mentions)
Linoleic acid, by Merck Group (1 mentions)
7 protocols using nα benzoyl dl arginine p nitroanilide
1
Purification and Characterization of Enzymes from Yellow Bell Pepper
2
Trypsin Purification and Activity Assay
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N-α-Benzoyl-DL-arginine-p-nitroanilide (BApNA), soybean trypsin inhibitor (SBTI), Bovine serum albumin (BSA), acrylamide, bis-acrylamide, and other electrophoretic reagents were procured from Sigma Chemical Co. (St. Louis, Mo, USA). Sephadex G-75 was purchased from Amersham Biosciences (Uppsala, Sweden). Trypsin-Sepharose CL-4B, low molecular weight markers and azocasein were purchased from Sisco Research Limited (Mumbai, India). All other chemicals and reagents used were of analytical grade.
3
Extraction and Characterization of Garlic Trypsin
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Allium sativum (PUSA- AG 102) commonly known as “garlic” was obtained from IARI, New Delhi. Chemicals; trypsin (bovine pancreatic trypsin), Nα-benzoyl-DL-arginine-p-nitroanilide (BAPNA), phenylmethylsulfonyl fluoride (PMSF), Polyvinylpyrrolidone (PVP), acrylamide, bis-acrylamide, Tetramethylethylenediamine (TEMED), ammonium persulfate and Sodium Dodecyl Sulfate (SDS), acrylamide, bis-acrylamide, TEMED, ammonium persulfate and SDS were obtained from Sigma-Aldrich. All other reagents and chemicals used were of analytical grade.
4
Enzyme Activity and Inhibitor Assays
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α-amylase [EC 3.2.1.1; 4-α-D-glucan 4-glucanohydrolase], xanthine oxidase [EC 1.17.3.2, xanthine:oxygen oxidoreductase], lipoxygenase [EC 1.13.11.34, arachidonate: oxygen 5-oxidoreductase], chymotrypsin [EC 3.4.21.1], trypsin [EC 3.4.21.4], N-α-Benzoyl-DL-Arginine p-Nitroanilide (BAPNA), N-Glutaryl-L-Phenylalanine p-Nitroanilide (GPNA), furosemide, Aldactone (containing spironolactone as active compound), linoleic acid, iodine reagent, sodium phosphate, Tween 20, the amino acid kit containing standard amino-acids (≥99%), and cystine were purchased from Sigma-Aldrich.
5
Immobilization of Trypsin on Agarose Beads
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Agarose 6BCL was acquired from GE Healthcare Bio-Sciences (Uppsala, Sweden) and corn cob powder from SAGRAN (Industry of Animal Feed Ingredients Ltd., Salto Grande, Brazil), Trypsin (EC 3.4.21.4), N-α-benzoyl-DL-arginine-p-nitroanilide (BAPNA), benzamidine hydrochloride, 2,3-epoxy-1-propanol, 1,2-ethanodiamine (EDA), glutaraldehyde, sodium periodate (NaIO4), sodium borohydride (NaBH4), iminodiacetic acid (IDA) and 2,4,6-trinitrobenzene sulfonic acid (TNBS) were purchased from Sigma-Aldrich (St. Louis, MO, USA).
6
Biofortification of Pearl Millet
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Bovine pancreatic trypsin, bovine pancreatic chymotrypsin, papain from papaya tree latex, and bromelain from pineapple stem were procured from Sisco Research Laboratory (Mumbai, India). Bovine serum albumin (BSA), ficin (fig tree latex), N-α-benzoyl-dl-arginine-p-nitroanilide (BApNA), N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide (SAApNA), pGlu-Phe-Leu-p-nitroanilide (pFLNA), N-acetyl-d-glucosamine, laminarin, crab shell chitin, and dithiotheitol (DTT) were purchased from Sigma (St. Louis, MO). Glucose estimation kit procured from Kamineni Life Sciences, Hyderabad. X-ray films were purchased from Carestream Health India Pvt Ltd. (Mumbai). All other chemicals and reagents used were of analytical grade. 1). All these lines were biofortified using classical recombinant breeding approaches (Govindaraj et al. 2019a) . Briefly, biofortification was achieved by crossing among the high Fe/Zn lines and later to the elite lines followed by pedigree breeding to fix the line with high Fe/Zn in agronomically superior backgrounds at F 6 and later stages. These micronutrients are highly heritable and predominantly controlled by additive genes, and therefore, it is highly feasible to breed biofortified lines in pearl millet. Pearl millet biofortification breeding approaches are well described elsewhere (Rai et al. 2012; Govindaraj et al. 2013 Govindaraj et al. , 2019b)) .
7
Measuring Gut Protease Activities
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Total protease activity was determined by using azocasein as a substrate [19] . The gut extract was mixed with the substrate and incubated for 50 min. Then, 200 μl of 5 % TCA was added and centrifuged. To the supernatant, equal volumes of 1 N NaOH were added and absorbance was read at 450 nm. Units for total protease activity (UA) were calculated by using the equation unit activity (UA)=ABS 450 nm/[time (min)×volume of enzyme (ml)]. Trypsin activity was measured by incubating the gut extract with Nα-benzoyl-DL-arginine pnitroanilide (Sigma-Aldrich), and chymotrypsin activity was measured by incubating the gut extract with N-glutaryl-L-phenylalanine p-nitroanilide (Sigma-Aldrich) [20] . Elastase activity of H. armigera gut proteases was measured by incubating the gut extract with N-succinylalanine-alanine-alanine p-nitroanilide (Sigma-Aldrich) [21] . The gut extract was mixed with respective substrates and incubated for 20 min at 37 °C. Then, 300 μl of 30 % acetic acid was added and stand for 10 min. The samples were centrifuged, and absorbance was read at 410 nm using UV-visible spectrophotometer (Hitachi U-2900, Japan). One unit of enzyme activity was defined as the amount of enzyme catalyzing the hydrolysis of 1 μmol substrate per minute at 30 °C.
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