Improvement of lactoferrin thermal stability by complex coacervation using soy soluble polysaccharides

نویسندگان

چکیده

Lactoferrin (LF) is a multifunctional protein in the transferrin family that has been widely used food and pharmaceutical products. However, it susceptible to denaturation during thermal processing, which can diminish functionality bioavailability of LF final product. Coacervation with biopolymers demonstrated as promising approach protect from denaturation. This work aims study formation conditions, structural characteristics, interaction mechanisms soy soluble polysaccharides (SSP) lactoferrin coacervate complex (SSP-LF), investigate effect SSP-LF on changes antimicrobial capacity before after treatment. Either insoluble complexes could be formed depending pH (4–7) ratios (SSP: = 8:1 1:16), according turbidity, zeta-potential, particle size analysis. Electrophoresis, SEM, FTIR, CD spectra measurement suggested maintain secondary structures LF. Quartz crystal microbalance dissipation (QCM-D) was elucidate real-time interactions between SSP LF, showing major driving force form electrostatic interaction. The able prevent aggregation/denaturation loss ?-helix treatment at neutral pH. maintained improved stability facilitate application various commercial

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Complex Coacervation of Soy Proteins, Isoflavones and Chitosan.

In this study, the chitosan-induced coacervation of soy protein-isoflavone complexes in soymilk was investigated. Most of the soymilk proteins, including β-conglycinin (7S), glycinin (11S), and isoflavones, were found to coacervate into the soymilk pellet fraction (SPF) following the addition of 0.5% chitosan. The total protein in the soymilk supernatant fraction (SSF) decreased from 18.1 ± 0.3...

متن کامل

Heteroprotein complex coacervation: bovine β-lactoglobulin and lactoferrin.

Lactoferrin (LF) and β-lactoglobulin (BLG), strongly basic and weakly acidic bovine milk proteins, form optically clear coacervates under highly limited conditions of pH, ionic strength I, total protein concentration C(P), and BLG:LF stoichiometry. At 1:1 weight ratio, the coacervate composition has the same stoichiometry as its supernatant, which along with DLS measurements is consistent with ...

متن کامل

Improvement of Thermal Stability of BCG Vaccine

Background: Thermal stability (TS) is a part of the BCG vaccine characterization by which the consistency of process in BCG vaccine production could be confirmed. To enhance the TS of the vaccine, some prevalent stabilizers in different concentrations were added to the final formulation of BCG bulk prior to Freeze-drying process. We found a formulation more effective than the current stabilizer...

متن کامل

improvement of thermal stability of dfpase by in silico methods

efficiency of enzymes which are used in industrial or environmental applications is highly dependent on their thermal stability. in this study, the stability of dfpase has been evaluated after introducing disulfide bonds to the structure. the results obtained from a series of protein design software were subjected to molecular dynamics simulation at different temperature to test the performance...

متن کامل

‏‎suppression of coke formation in thermal cracking by coke inhibitors‎‏

‏‎the main purpose of this research was to:1.develop a coking model for thermal cracking of naphtha.2.study coke inhibition methods using different coke inhibitors.developing a coking model in naphtha cracking reactors requires a suitable model of the thermal cracking reactor based on a reliable kinetic model.to obtain reliable results all these models shall be solved simultaneously.for this pu...

15 صفحه اول

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Food Hydrocolloids

سال: 2022

ISSN: ['1873-7137', '0268-005X']

DOI: https://doi.org/10.1016/j.foodhyd.2022.107736