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      Seed Protein of Lentils: Current Status, Progress, and Food Applications

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          Abstract

          Grain legumes are widely recognized as staple sources of dietary protein worldwide. Lentil seeds are an excellent source of plant-based proteins and represent a viable alternative to animal and soybean proteins for food processing formulations. Lentil proteins provide not only dietary amino acids but are also a source of bioactive peptides that provide health benefits. This review focuses on the current knowledge of seed protein, extraction and isolation methods, bioactive peptides, and food applications of lentil protein. Lentil is the most rapidly expanding crop for direct human consumption, and has potential for greater impact as a protein source for food processing applications. Improvements in lentil protein quality, amino acid composition, and processing fractions will enhance the nutritional quality of this rapidly expanding crop globally.

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          Protein content and amino acid composition of commercially available plant-based protein isolates

          Stefan Gorissen, Julie Crombag, Joan M G Senden … (2018)
          The postprandial rise in essential amino acid (EAA) concentrations modulates the increase in muscle protein synthesis rates after protein ingestion. The EAA content and AA composition of the dietary protein source contribute to the differential muscle protein synthetic response to the ingestion of different proteins. Lower EAA contents and specific lack of sufficient leucine, lysine, and/or methionine may be responsible for the lower anabolic capacity of plant-based compared with animal-based proteins. We compared EAA contents and AA composition of a large selection of plant-based protein sources with animal-based proteins and human skeletal muscle protein. AA composition of oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, potato, milk, whey, caseinate, casein, egg, and human skeletal muscle protein were assessed using UPLC–MS/MS. EAA contents of plant-based protein isolates such as oat (21%), lupin (21%), and wheat (22%) were lower than animal-based proteins (whey 43%, milk 39%, casein 34%, and egg 32%) and muscle protein (38%). AA profiles largely differed among plant-based proteins with leucine contents ranging from 5.1% for hemp to 13.5% for corn protein, compared to 9.0% for milk, 7.0% for egg, and 7.6% for muscle protein. Methionine and lysine were typically lower in plant-based proteins (1.0 ± 0.3 and 3.6 ± 0.6%) compared with animal-based proteins (2.5 ± 0.1 and 7.0 ± 0.6%) and muscle protein (2.0 and 7.8%, respectively). In conclusion, there are large differences in EAA contents and AA composition between various plant-based protein isolates. Combinations of various plant-based protein isolates or blends of animal and plant-based proteins can provide protein characteristics that closely reflect the typical characteristics of animal-based proteins.
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              Food protein-derived bioactive peptides: production, processing, and potential health benefits.

              Chibuike Udenigwe, Rotimi E. Aluko (2011)
              Bioactive peptides (BAPs), derived through enzymatic hydrolysis of food proteins, have demonstrated potential for application as health-promoting agents against numerous human health and disease conditions, including cardiovascular disease, inflammation, and cancer. The feasibility of pharmacological application of these peptides depends on absorption and bioavailability in intact forms in target tissues, which in turn depends on structure of the peptides. Therefore, production and processing of peptides based on important structure-function parameters can lead to the production of potent peptides. This article reviews the literature on BAPs with emphasis on strategic production and processing methods as well as antihypertensive, anticancer, anticalmodulin, hypocholesterolemic, and multifunctional properties of the food protein-derived peptides. It is recommended that future research efforts on BAP should be directed toward elucidation of their in vivo molecular mechanisms of action, safety at various doses, and pharmacological activity in maintaining homeostasis during aberrant health conditions in human subjects. © 2011 Institute of Food Technologists®
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                Author and article information

                Journal
                Journal ID (nlm-ta): Foods
                Journal ID (iso-abbrev): Foods
                Journal ID (publisher-id): foods
                Title: Foods
                Publisher: MDPI
                ISSN (Electronic): 2304-8158
                Publication date (Electronic): 04 September 2019
                Publication date Collection: September 2019
                Volume: 8
                Issue: 9
                Electronic Location Identifier: 391
                Affiliations
                [1 ]Department of Plant Sciences, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada (M.S.) (A.V.)
                [2 ]Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada
                [3 ]Institute of Food Science, Technology and Nutrition (ICTAN), Spanish National Research Council (CSIC), Jose Antonio Novais 10, 28040 Madrid, Spain (C.M.-V.) (J.F.)
                Author notes
                [* ]Correspondence: hamid.khazaei@ 123456usask.ca or hamid.khazaei@ 123456gmail.com ; Tel.: +1-306-966-5859
                [†]

                Current address: Agriculture and Agri-Food Canada, Lethbridge, AB T1J 4B1, Canada.

                Author information
                https://orcid.org/0000-0002-5202-8764
                https://orcid.org/0000-0002-1155-6464
                Article
                Publisher ID: foods-08-00391
                DOI: 10.3390/foods8090391
                PMC ID: 6769807
                PubMed ID: 31487958
                SO-VID: 593f8a88-aff0-488d-ba60-b004867c2d2a
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 20 July 2019
                Date accepted : 30 August 2019
                Categories
                Subject: Review

                Keywords: lens,protein,amino acid,legume,functionality,bioactive peptides
                Data availability:
                Keywords: lens, protein, amino acid, legume, functionality, bioactive peptides

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