Source: PENNSYLVANIA STATE UNIVERSITY submitted to NRP
PCHI: RE-STRUCTURING PULSE PROTEINS INTO VALUABLE FIBRILS VIA BIOCATALYSIS
Sponsoring Institution
Agricultural Research Service/USDA
Project Status
ACTIVE
Funding Source
Reporting Frequency
Annual
Accession No.
0445002
Grant No.
(N/A)
Cumulative Award Amt.
(N/A)
Proposal No.
(N/A)
Multistate No.
(N/A)
Project Start Date
Sep 1, 2023
Project End Date
Dec 31, 2025
Grant Year
(N/A)
Program Code
[(N/A)]- (N/A)
Recipient Organization
PENNSYLVANIA STATE UNIVERSITY
(N/A)
PENNSYLVANIA,PA 16202
Performing Department
(N/A)
Non Technical Summary
(N/A)
Animal Health Component
0%
Research Effort Categories
Basic
0%
Applied
0%
Developmental
100%
Classification

Knowledge Area (KA)Subject of Investigation (SOI)Field of Science (FOS)Percent
2041410101040%
5021412101030%
2041414101030%
Goals / Objectives
In this project, we will re-structure the globular pulse proteins into fibrils via novel and sustainable biocatalysis techniques. We will further study the fibrillation attributes that can guide their novel and future applications. To achieve these goals, three objectives will be undertaken: (1) Optimize the biocatalytic generation of fibril precursors from pulse proteins; (2) Induce the formation of protein fibrils under specific biological treatments; and (3) Determine the digestibility, allergenicity, and functionality of pulse protein fibrils.
Project Methods
To achieve Objective 1, we will perform pulse protein extraction using enzyme-assisted extraction method and conduct the preparation of fibril precursors with desired functions via optimized enzymatic hydrolysis. The protein hydrolysates that have the highest beta-sheet content and hydrophobicity will be selected from each pulse source. To achieve objective 2, we will perform pulse protein fibril formation via non-enzymatic (change in pH and heating) versus enzymatic inductions. Afterward, we will perform the characterization and comparison of the fibrils for fibril formation, composition of protein subunits, morphological features, average particle sizes, and secondary structures. The protein fibrils that have the highest fibril formation, uniform protein subunits, size, and structures, and ordered fibrillar morphological features will be selected. To achieve objective 3, we will perform digestion of pulse protein fibrils in a simulated gastrointestinal digestion model. Pulse proteins, pulse protein non-digested fibrils, gastric digests of fibrils, and intestinal digests of fibrils, will be used for the following assays: digestibility assay, allergenicity assay, and functionality assay.