Increasing Methionine in the Lectin Erythroagglutanin (PHA‐E) of Phaseolus vulgaris (Black Bean)

Abstract

Many developing countries around the world do not have access to regular sources of protein (e.g. meats, fish, dairy products, etc). Beans have become a staple food in many of these communities' diets for their daily protein and calorie intake due to their availability. This crop is a great agronomic choice because it requires minimal inputs. It can be grown at small and large‐scale farms. Though it is a reliable source of protein, the most abundant proteins are low in an essential amino acid, methionine. Nutritional deficiencies can be attributed to the two major stores of protein in the bean, phaseolin and lectin; Lectin is the second most abundant seed protein. Its biochemical characteristics make it an effective anti‐herbivory agent, and if the beans are not prepared properly, lectin can affect the nutritional value. We selected several sites containing isoleucine to convert to methionine in the common black bean to improve the methionine content. Plasmids were prepared and transformed into wild type plants using Agrobacterium. The gene cassette was created and successfully introduced into T0 plants. The putative transformants were tested to confirm they carry the expected modified gene using PCR. The positive plants were allowed to grow, and their seeds were collected. The T1 plants are being tested for the expression and accumulation of PHA‐E. We will begin to investigate how the conversion of isoleucine to methionine affects the structure and function of the PHA‐E protein lectin. This research could elucidate whether we can improve the nutritional value of essential foods in third world countries.Support or Funding InformationThis research was made possible by funding through the NIH grant #GM063787.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.