{"title":"Composite Gelation of Pea Protein and Gellan Gum: Rheological Characterization and Potential Application in Controlled In-Vitro Release of α-Amylase","authors":"Somnath Basak, Rekha S. Singhal","doi":"10.1007/s11483-025-09970-x","DOIUrl":null,"url":null,"abstract":"<div><p>Chronic pancreatitis is often associated with a decreased secretion of α-amylase by the pancreas. Hence, oral administration of α-amylase becomes essential; however, only a small portion of the enzyme reaches the duodenum due to inactivation of the enzyme in the gastric environment. Hence, composite gelation of pea protein and gellan [high-acyl (PP_HAG)] and [low-acyl (PP_LAG)] was studied in the presence of glucono-δ-lactone (GDL) to encapsulate and protect α-amylase from the gastric environment and facilitate a controlled in-vitro release in the intestine. The sole pea protein gel (PP) was fabricated by the pH shift and transglutaminase treatment. The pH of composite gelation was around 3.0-3.5, inducing electrostatic interactions between pea protein and gellan. Hydrogen and ionic bonds were observed in composite gels, while hydrophobic interactions were predominant in PP. A higher water holding capacity and a lower pore size, crystallinity and swelling index were observed in the composite gels. PP_HAG exhibited greater swelling in simulated gastric fluid (SGF) than in simulated intestinal fluid (SIF), while PP_LAG exhibited greater swelling in SIF. Although PP resulted in a spurt release of α-amylase, PP_LAG resulted in a sustained release in the SGF. PP_HAG on the other hand, efficiently protected α-amylase from gastric conditions and facilitated a controlled release in SIF.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":"20 2","pages":""},"PeriodicalIF":2.8000,"publicationDate":"2025-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-025-09970-x","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Chronic pancreatitis is often associated with a decreased secretion of α-amylase by the pancreas. Hence, oral administration of α-amylase becomes essential; however, only a small portion of the enzyme reaches the duodenum due to inactivation of the enzyme in the gastric environment. Hence, composite gelation of pea protein and gellan [high-acyl (PP_HAG)] and [low-acyl (PP_LAG)] was studied in the presence of glucono-δ-lactone (GDL) to encapsulate and protect α-amylase from the gastric environment and facilitate a controlled in-vitro release in the intestine. The sole pea protein gel (PP) was fabricated by the pH shift and transglutaminase treatment. The pH of composite gelation was around 3.0-3.5, inducing electrostatic interactions between pea protein and gellan. Hydrogen and ionic bonds were observed in composite gels, while hydrophobic interactions were predominant in PP. A higher water holding capacity and a lower pore size, crystallinity and swelling index were observed in the composite gels. PP_HAG exhibited greater swelling in simulated gastric fluid (SGF) than in simulated intestinal fluid (SIF), while PP_LAG exhibited greater swelling in SIF. Although PP resulted in a spurt release of α-amylase, PP_LAG resulted in a sustained release in the SGF. PP_HAG on the other hand, efficiently protected α-amylase from gastric conditions and facilitated a controlled release in SIF.
期刊介绍:
Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell.
A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.