Soybean Bioactive Peptides and Their Functional Properties
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Variations Through the Day of Hepatic and Muscular Cathepsin A
Downloaded from Br. J. Nutr. (1980), 4,61 61 https://www.cambridge.org/core Variations through the day of hepatic and muscular cathepsin A (carboxypeptidase A; EC 3.4.12.2), C (dipeptidyl peptidase; EC 3.4.14.1) and D (endopeptidase D ;EC 3.4.23.5) activities and free amino acids of blood in rats: influence of feeding schedule . IP address: BY CHRISTIANE OBLED, M. ARNAL AND C. VALIN* 170.106.40.139 Laboratoire &Etude du MPtabolisme Azott!, INRA Theix-63I 10 Beaumont, France (Received 17 April 1978 - Accepted 4 January 1980) , on I. Growing rats were fed either ad lib. or with six (equal) meals offered every 4 h (from 10.00 hours). Rats 02 Oct 2021 at 01:32:10 of each group were killed at intervals of 4 h beginning at I 1.00 hours. Activities of cathepsin A (carboxy- peptidase A; EC3.4.1z.z), C (dipeptidyl peptidase; EC3.4.14.1) and D (endopeptidaseD EC3.4.23.5) were measured in liver and muscle homogenates and free amino acids in blood were determined. 2. In the rats fed ad lib. activities of carboxypeptidase A and endopeptidase D in liver and muscle showed significant variation, with maximum activity in the light period. In general, meal-feeding only caused minor differences in cathepsin activities; although significant differences occurred for carboxypeptidase A. For the latter enzyme a peak in activity occurred in the dark as well as in the light period. 3. Irrespective of the feeding schedule, the lower concentration of free essential amino acids of blood , subject to the Cambridge Core terms of use, available at occurred generally during the night period. -
Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: a Review
International Journal of Molecular Sciences Review Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review Rui Liu 1,2,3,4 , Jianming Cheng 1,2,3,* and Hao Wu 1,2,3,* 1 Jiangsu Key Laboratory of Research and Development in Marine Bio-resource Pharmaceutics, Nanjing University of Chinese Medicine, Nanjing 210023, China; [email protected] 2 Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine, Nanjing 210023, China 3 School of Pharmacy, Nanjing University of Chinese Medicine, Nanjing 210023, China 4 School of Pharmacy, University of Wisconsin-Madison, Madison, WI 53705, USA * Correspondence: [email protected] (J.C.); [email protected] (H.W.); Tel.: +86-25-85811524 (J.C.); +86-25-85811206 (H.W.) Received: 21 December 2018; Accepted: 19 January 2019; Published: 22 January 2019 Abstract: Diabetes is a chronic metabolic disorder which leads to high blood sugar levels over a prolonged period. Type 2 diabetes mellitus (T2DM) is the most common form of diabetes and results from the body’s ineffective use of insulin. Over ten dipeptidyl peptidase IV (DPP-IV) inhibitory drugs have been developed and marketed around the world in the past decade. However, owing to the reported adverse effects of the synthetic DPP-IV inhibitors, attempts have been made to find DPP-IV inhibitors from natural sources. Food-derived components, such as protein hydrolysates (peptides), have been suggested as potential DPP-IV inhibitors which can help manage blood glucose levels. This review focuses on the methods of discovery of food-derived DPP-IV inhibitory peptides, including fractionation and purification approaches, in silico analysis methods, in vivo studies, and the bioavailability of these food-derived peptides. -
Effect of Sourdough Fermentation on Lunasin-Like Polypeptides
Rizzello et al. Microb Cell Fact (2015) 14:168 DOI 10.1186/s12934-015-0358-6 RESEARCH Open Access Italian legumes: effect of sourdough fermentation on lunasin‑like polypeptides Carlo Giuseppe Rizzello1*, Blanca Hernández‑Ledesma2, Samuel Fernández‑Tomé2, José Antonio Curiel1, Daniela Pinto3, Barbara Marzani3, Rossana Coda4 and Marco Gobbetti1 Abstract Background: There is an increasing interest toward the use of legumes in food industry, mainly due to the qual‑ ity of their protein fraction. Many legumes are cultivated and consumed around the world, but few data is available regarding the chemical or technological characteristics, and especially on their suitability to be fermented. Never‑ theless, sourdough fermentation with selected lactic acid bacteria has been recognized as the most efficient tool to improve some nutritional and functional properties. This study investigated the presence of lunasin-like polypeptides in nineteen traditional Italian legumes, exploiting the potential of the fermentation with selected lactic acid bacteria to increase the native concentration. An integrated approach based on chemical, immunological and ex vivo (human adenocarcinoma Caco-2 cell cultures) analyses was used to show the physiological potential of the lunasin-like polypeptides. Results: Italian legume varieties, belonging to Phaseulus vulgaris, Cicer arietinum, Lathyrus sativus, Lens culinaris and Pisum sativum species, were milled and flours were chemically characterized and subjected to sourdough fermenta‑ tion with selected Lactobacillus plantarum C48 and Lactobacillus brevis AM7, expressing different peptidase activities. Extracts from legume doughs (unfermented) and sourdoughs were subjected to western blot analysis, using an anti- lunasin primary antibody. Despite the absence of lunasin, different immunoreactive polypeptide bands were found. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
CD13/Aminopeptidase N Is a Potential Therapeutic Target for Inflammatory Disorders Chenyang Lu,*,† Mohammad A
CD13/Aminopeptidase N Is a Potential Therapeutic Target for Inflammatory Disorders Chenyang Lu,*,† Mohammad A. Amin,* and David A. Fox* CD13/aminopeptidase N is a widely expressed ectoen- and processing of inflammatory mediators, which are im- zyme with multiple functions. As an enzyme, CD13 portant features of immune responses. In this study, we regulates activities of numerous cytokines by cleaving review evidence concerning the involvement of CD13, includ- their N-terminals and is involved in Ag processing by ing a soluble form of the molecule in inflammation and its trimming the peptides bound to MHC class II. Inde- potential as a therapeutic target in inflammatory disorders. pendent of its enzymatic activity, cell membrane CD13 functions by cross-linking–induced signal transduc- Mechanisms of CD13 functions tion, regulation of receptor recycling, enhancement of CD13 was named aminopeptidase N because of its prefer- FcgR-mediated phagocytosis, and acting as a receptor ence for binding neutral amino acids and because it removes for cytokines. Moreover, soluble CD13 has multiple N-terminal amino acids from unsubstituted oligopeptides, proinflammatory roles mediated by binding to G-pro- with the exception of peptides with proline in the penulti- tein–coupled receptors. CD13 not only modulates de- mate position (11). By cleaving N termini, CD13 regulates velopment and activities of immune-related cells, but activity of numerous hormones,cytokines,andchemokines also regulates functions of inflammatory mediators. that participate in inflammation. Moreover, CD13 is coex- Therefore, CD13 is important in the pathogenesis of pressed by MHC class II (MHC II)–bearing APCs (12), and is various inflammatory disorders. Inhibitors of CD13 involved in the trimming of MHC II–associated peptides on the have shown impressive anti-inflammatory effects, but surface of APCs (5, 13, 14) (Fig. -
Regulation of Intestinal Inflammation by Soybean and Soy-Derived Compounds
foods Review Regulation of Intestinal Inflammation by Soybean and Soy-Derived Compounds Abigail Raffner Basson 1,2,* , Saleh Ahmed 2, Rawan Almutairi 3, Brian Seo 2 and Fabio Cominelli 1,2 1 Division of Gastroenterology & Liver Diseases, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA; [email protected] 2 Digestive Health Research Institute, University Hospitals Cleveland Medical Center, Cleveland, OH 44106, USA; [email protected] (S.A.); [email protected] (B.S.) 3 Department of Pathology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA; [email protected] * Correspondence: [email protected] Abstract: Environmental factors, particularly diet, are considered central to the pathogenesis of the inflammatory bowel diseases (IBD), Crohn’s disease and ulcerative colitis. In particular, the Westernization of diet, characterized by high intake of animal protein, saturated fat, and refined carbohydrates, has been shown to contribute to the development and progression of IBD. During the last decade, soybean, as well as soy-derived bioactive compounds (e.g., isoflavones, phytosterols, Bowman-Birk inhibitors) have been increasingly investigated because of their anti-inflammatory properties in animal models of IBD. Herein we provide a scoping review of the most studied disease mechanisms associated with disease induction and progression in IBD rodent models after feeding of either the whole food or a bioactive present in soybean. Keywords: inflammatory bowel disease; isoflavone; bioactive compound; isoflavones; inflammation; Crohn’s disease; western diet; plant-based Citation: Basson, A.R.; Ahmed, S.; Almutairi, R.; Seo, B.; Cominelli, F. Regulation of Intestinal Inflammation by Soybean and Soy-Derived Compounds. Foods 2021, 10, 774. -
(12) Patent Application Publication (10) Pub. No.: US 2006/0110747 A1 Ramseier Et Al
US 200601 10747A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2006/0110747 A1 Ramseier et al. (43) Pub. Date: May 25, 2006 (54) PROCESS FOR IMPROVED PROTEIN (60) Provisional application No. 60/591489, filed on Jul. EXPRESSION BY STRAIN ENGINEERING 26, 2004. (75) Inventors: Thomas M. Ramseier, Poway, CA Publication Classification (US); Hongfan Jin, San Diego, CA (51) Int. Cl. (US); Charles H. Squires, Poway, CA CI2O I/68 (2006.01) (US) GOIN 33/53 (2006.01) CI2N 15/74 (2006.01) Correspondence Address: (52) U.S. Cl. ................................ 435/6: 435/7.1; 435/471 KING & SPALDING LLP 118O PEACHTREE STREET (57) ABSTRACT ATLANTA, GA 30309 (US) This invention is a process for improving the production levels of recombinant proteins or peptides or improving the (73) Assignee: Dow Global Technologies Inc., Midland, level of active recombinant proteins or peptides expressed in MI (US) host cells. The invention is a process of comparing two genetic profiles of a cell that expresses a recombinant (21) Appl. No.: 11/189,375 protein and modifying the cell to change the expression of a gene product that is upregulated in response to the recom (22) Filed: Jul. 26, 2005 binant protein expression. The process can improve protein production or can improve protein quality, for example, by Related U.S. Application Data increasing solubility of a recombinant protein. Patent Application Publication May 25, 2006 Sheet 1 of 15 US 2006/0110747 A1 Figure 1 09 010909070£020\,0 10°0 Patent Application Publication May 25, 2006 Sheet 2 of 15 US 2006/0110747 A1 Figure 2 Ester sers Custer || || || || || HH-I-H 1 H4 s a cisiers TT closers | | | | | | Ya S T RXFO 1961. -
The Microbiota-Produced N-Formyl Peptide Fmlf Promotes Obesity-Induced Glucose
Page 1 of 230 Diabetes Title: The microbiota-produced N-formyl peptide fMLF promotes obesity-induced glucose intolerance Joshua Wollam1, Matthew Riopel1, Yong-Jiang Xu1,2, Andrew M. F. Johnson1, Jachelle M. Ofrecio1, Wei Ying1, Dalila El Ouarrat1, Luisa S. Chan3, Andrew W. Han3, Nadir A. Mahmood3, Caitlin N. Ryan3, Yun Sok Lee1, Jeramie D. Watrous1,2, Mahendra D. Chordia4, Dongfeng Pan4, Mohit Jain1,2, Jerrold M. Olefsky1 * Affiliations: 1 Division of Endocrinology & Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. 2 Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 3 Second Genome, Inc., South San Francisco, California, USA. 4 Department of Radiology and Medical Imaging, University of Virginia, Charlottesville, VA, USA. * Correspondence to: 858-534-2230, [email protected] Word Count: 4749 Figures: 6 Supplemental Figures: 11 Supplemental Tables: 5 1 Diabetes Publish Ahead of Print, published online April 22, 2019 Diabetes Page 2 of 230 ABSTRACT The composition of the gastrointestinal (GI) microbiota and associated metabolites changes dramatically with diet and the development of obesity. Although many correlations have been described, specific mechanistic links between these changes and glucose homeostasis remain to be defined. Here we show that blood and intestinal levels of the microbiota-produced N-formyl peptide, formyl-methionyl-leucyl-phenylalanine (fMLF), are elevated in high fat diet (HFD)- induced obese mice. Genetic or pharmacological inhibition of the N-formyl peptide receptor Fpr1 leads to increased insulin levels and improved glucose tolerance, dependent upon glucagon- like peptide-1 (GLP-1). Obese Fpr1-knockout (Fpr1-KO) mice also display an altered microbiome, exemplifying the dynamic relationship between host metabolism and microbiota. -
Cloning of the Prolyl-Dipeptidyl-Peptidase from Aspergillus Oryzae
Patentamt Europaisches ||| || 1 1| || || || || || || || || ||| || (19) J European Patent Office Office europeen des brevets (11) EP 0 897 012 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) int. CI.6: C12N 15/57, C12N 9/48, 17.02.1999 Bulletin 1999/07 C12N 1/15, C12N 1/19, (21) Application number: 97111377.4 C12P 21/06, A23J 3/30 (22) Date of filing: 05.07.1997 (84) Designated Contracting States: • Doumas, Agnes AT BE CH DE DK ES Fl FR GB GR IE IT LI LU MC 1124 Gollion (CH) NL PT SE • Affolter, Michael Designated Extension States: 1009 Pully (CH) AL LT LV RO SI • Van Den Broek Epalinges (CH) (71) Applicant: SOCIETE DES PRODUITS NESTLE S.A. (74) Representative: 1800 Vevey (CH) Straus, Alexander, Dr. Dipl.-Chem. et al KIRSCHNER & KURIG (72) Inventors: Patentanwalte • Monod, Michel Sollner Strasse 38 1 01 2 Lausanne (CH) 81 479 Munchen (DE) (54) Cloning of the prolyl-dipeptidyl-peptidase from aspergillus oryzae (57) The invention has for object the new recom- lysate obtainable by fermentation with at least a micro- binant prolyl-dipeptidyl-peptidase enzyme (DPP IV) oganism providing a prolyl-dipeptidyl-peptidase activity from Aspergillus oryzae comprising the amino-acid higher than 50 mU per ml when grown in a minimal sequence from amino acid 1 to amino acid 755 of SEQ medium containing 1 % (w/v) of wheat gluten. ID NO:2 or functional derivatives thereof, and providing a high level of hydrolysing specificity towards proteins and peptides starting with X-Pro- thus liberating dipep- tides of X-Pro type, wherein X is any amino-acid. -
Partial Characterisation of Dipeptidyl Peptidase 4 (DP 4
Partial Characterisation of Dipeptidyl Peptidase 4 (DP 4) for the Treatment of Type 2 Diabetes and its Identification as a novel Pharmaceutical Target for Stress-related Indications Beiträge zur Charakterisierung der Dipeptidylpeptidase 4 (DP 4) für die Behandlung von Typ-2-Diabetes und deren Identifizierung als ein neuartiges pharmazeutisches Ziel für stressvermittelte Indikationen Der Naturwissenschaftlichen Fakultät der Friedrich-Alexander-Universität Erlangen-Nürnberg zur Erlangung des Doktorgrades Dr. rer. nat. vorgelegt von M. Sc. (Biochemie) Leona Wagner aus Rheinfelden (Baden) Als Dissertation genehmigt von der Naturwissenschaftlichen Fakultät der Friedrich-Alexander-Universität Erlangen-Nürnberg Tag der mündlichen Prüfung: 23.10.2012 Vorsitzender der Promotionskommission: Prof. Dr. Rainer Fink Erstberichterstatter: Prof. Dr. med. Stephan von Hörsten Zweitberichterstatter: Prof. Dr. Johann Helmut Brandstätter Publications, Presentations and Posters Part of the present study have been published or submitted in the following journals or presented on the following conferences: Publications: 1. Hinke, S.A., McIntosh, C.H., Hoffmann, T., Kuhn-Wache, K., Wagner, L., Bar, J., Manhart, S., Wermann, M., Pederson, R.A., and Demuth, H.U. (2002) On combination therapy of diabetes with metformin and dipeptidyl peptidase IV inhibitors. Diabetes Care 25, 1490- 1491. 2. Bär, J., Weber, A., Hoffmann, T., Stork, J., Wermann, M., Wagner, L., Aust, S., Gerhartz, B., and Demuth, H.U. (2003) Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. A structural and mechanistic comparison between the recombinant human and the purified porcine enzyme. Biol. Chem. 384, 1553-1563. 3. Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R., Huber, R., Bode, W., Demuth, H.U., and Brandstetter, H. -
The Effect of Lunasin from Indonesian Soybean Extract on Inducible Nitric Oxide Synthase and Β-Catenin Expression in Dextran Sodium Sulfate-Induced Mice Colon
Online - 2455-3891 Vol 11, Issue 1, 2018 Print - 0974-2441 Research Article THE EFFECT OF LUNASIN FROM INDONESIAN SOYBEAN EXTRACT ON INDUCIBLE NITRIC OXIDE SYNTHASE AND β-CATENIN EXPRESSION IN DEXTRAN SODIUM SULFATE-INDUCED MICE COLON KUSMARDI KUSMARDI1, NESSA NESSA2*, ARI ESTUNINGTYAS2, ARYO TEDJO3, PUSPITA EKA WUYUNG1 1Department of Anatomical Pathology, Faculty of Medicine, Universitas Indonesia, Indonesia. 2Department of Pharmacology and Therapeutic, Faculty of Medicine, Universitas Indonesia, Indonesia. 3Department of Chemical Medicine, Faculty of Medicine, Universitas Indonesia, Indonesia. Email: [email protected] Received: 04 August 2017, Received and Accepted: 23 September 2017 ABSTRACT Objective: Inflammatory bowel diseases are idiopathic inflammatory disorders of the gastrointestinal tract. Chronic inflammation that occurs in the colon can develop into colon cancer. Lunasin has been known to resist inflammatory reactions induced by lipopolysaccharide in vitro. The role of lunasin as anti-inflammatory in vivo is not widely known. In this study, we analyzed the effect of lunasin from Indonesian soybean to decrease the risk Methods:of inflammation A total by of analyzing 30 mice theare expressionsdivided into of six inducible groups. nitricNormal oxide group synthase was not (iNOS) induced and byβ-catenin. dextran sodium sulfate (DSS). The other groups were induced by DSS 2% through drinking water for 9 days. After 9 days, negative group did not receive any treatment, besides the other groups received treatment given lunasin dose 20 mg/kg BB and 40 mg/kg BB, commercial lunasin, and positive given aspirin. Treatment was performed for 5 weeks. Results:Immunohistochemistry scores of iNOS and β-catenin proteins were analyzed using statistical tests. -
Lunasin and Bowman-Birk Protease Inhibitor Concentrations of Protein Extracts from Enzyme- Assisted Aqueous Extraction of Soybeans Juliana Maria L
Food Science and Human Nutrition Publications Food Science and Human Nutrition 5-31-2011 Lunasin and Bowman-Birk Protease Inhibitor Concentrations of Protein Extracts from Enzyme- Assisted Aqueous Extraction of Soybeans Juliana Maria L. Nobrega de Moura Iowa State University Blanca Hernandez-Ledesma University of California - Berkeley Neiva M. de Almeida Universidade Federal da Paraiba Chia-Chien Hsieh University of California - Berkeley Ben O. de Lumen UFonilvloerwsit ythi of sC andlifor anddia - itBerionkealley works at: http://lib.dr.iastate.edu/fshn_ag_pubs Part of the Agricultural Science Commons, Food Chemistry Commons, and the Plant Biology See next page for additional authors Commons The ompc lete bibliographic information for this item can be found at http://lib.dr.iastate.edu/ fshn_ag_pubs/100. For information on how to cite this item, please visit http://lib.dr.iastate.edu/ howtocite.html. This Article is brought to you for free and open access by the Food Science and Human Nutrition at Iowa State University Digital Repository. It has been accepted for inclusion in Food Science and Human Nutrition Publications by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Lunasin and Bowman-Birk Protease Inhibitor Concentrations of Protein Extracts from Enzyme-Assisted Aqueous Extraction of Soybeans Abstract Lunasin and Bowman-Birk protease inhibitor (BBI) are two soybean peptides to which health-promoting properties have been attributed. Concentrations of these peptides were determined in skim fractions produced by enzyme-assisted aqueous extraction processing (EAEP) of extruded full-fat soybean flakes (an alternative to extracting oil from soybeans with hexane) and compared with similar extracts from hexane- defatted soybean meal.