Digestibility and Enzymatic Activity in Vitro of Hen Egg White Lysozyme
ثبت نشده
چکیده
Objective: The aim of this study was to evaluate the protein digestibility and analyze the residual enzymatic activity of lysozyme. Methods: Protein digestibility was evaluated hydrolyzing the protein with pepsin at pH 1.2, 2.0, and 3.2 during 60, 90, and 120 minutes of incubation. These hydrolysates were analyzed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reversed-phase high-performance liquid chromatography. Residual enzymatic activity was evaluated with the spectrophotometric method at 450 nm. Results: Lysozyme was totally hydrolyzed with pepsin at pH 1.2. At pH 2.0, lysozyme was partially hydrolyzed and at pH 3.2 hydrolysis was absent at all times of the assay. Conclusions: Lysozyme was hydrolyzed with pepsin at low pH. Residual enzymatic method can be used to determine the grade of hydrolysis in lysozyme.
منابع مشابه
Inhibition of Amyloid Fibrils Formation from Hen Egg White Lysozyme by Satureia Hortensis Extract and its Effect on Learning and Spatial Memory of Rats
Background & Aims: Alzheimer's disease is a neurodegenerative disorder characterized by the abnormal aggregation of amyloid-β plaques in the brain. Although several studies have been done for finding effective medicines in the treatment of this disease, a drug that inhibits amyloid β aggregation and ameliorates the disorder has not been approved so far. One important therapeutic approach is use...
متن کاملStudy the Interaction of Ni Complex of Tetradentate Schiff Base Ligand with HEN Egg White Lysozyme
AbstractInteraction of Ni complex(Salen= N, N´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (HEWL) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. The protein binding affinity of Ni complex was found to be (3.0×103M−1). The binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 M...
متن کاملEffect of Cinnamomum Verum Extract on the Amyloid Formation of Hen Egg-white Lysozyme and Study of its Possible Role in Alzheimer’s Disease
Introduction: Diagnosing and treating diseases associated with amyloid fibers remain a great challenge despite of intensive research carried out. One important approach in the development of therapeutics is the use of herbal extracts which are rich in aromatic small molecules. Cinnamomum verum extract (CE) contains proanthocyanidin and cinnamaldehyde, which have been suggested to be capab...
متن کاملRedesign of the substrate-binding site of hen egg white lysozyme based on the molecular evolution of C-type lysozymes.
On the basis of the molecular evolution of hen egg white, human, and turkey lysozymes, three replacements (Trp62 with Tyr, Asn37 with Gly, and Asp101 with Gly) were introduced into the active-site cleft of hen egg white lysozyme by site-directed mutagenesis. The replacement of Trp62 with Tyr led to enhanced bacteriolytic activity at pH 6.2 and a lower binding constant for chitotriose. The fluor...
متن کاملInactivation of gram-negative bacteria by lysozyme, denatured lysozyme, and lysozyme-derived peptides under high hydrostatic pressure.
We have studied the inactivation of six gram-negative bacteria (Escherichia coli, Pseudomonas fluorescens, Salmonella enterica serovar Typhimurium, Salmonella enteritidis, Shigella sonnei, and Shigella flexneri) by high hydrostatic pressure treatment in the presence of hen egg-white lysozyme, partially or completely denatured lysozyme, or a synthetic cationic peptide derived from either hen egg...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2016