scholarly journals Chromatographic Profiles of Umami Fractions from Indonesian Commercial Salty Soy Sauce

2020 ◽  
Vol 16 (2) ◽  
pp. 36
Author(s):  
Hanifah Nuryani Lioe ◽  
Diana Ayu Nindita ◽  
Warsono El Kiyat
Keyword(s):  
Gel Filtration ◽  
Soy Sauce ◽  
Gel Filtration Chromatography ◽  
Hplc Chromatogram ◽  
Rp Hplc ◽  
Hplc Profiles ◽  
Taste Dilution Analysis ◽  
Chromatographic Profiles

Salty soy sauce subjected in this study is a variety of commercial soy products in Indonesia. Chromatographic profiles linked to taste dilution analysis of the soy sauce were analyzed by Sephadex G-15 gel filtration chromatography followed by RP-HPLC. The results showed that there were 4 umami fractions (Fractions I − IV) obtained by Sephadex G-15 separation. Chromatographic profiles at 254 nm could show the differentiation of the four fractions and then their RP-HPLC profiles were proven to be different from each other. Fraction III which contained 65% of the soy sauce dry matters, had the highest umami intensity with umami TD factor of 256, meanwhile, this fraction was tasted salty due to the salt contained in the soy sauce. Fraction III was dominated by the later peaks in the RP-HPLC chromatogram, which was more hydrophobic. The hydrophobic components were commonly tasted bitter, perhaps in the commercial salty soy sauce, the taste interaction between the umami and bitter components might have occurred.

scholarly journals Analysis of serum lipoproteins by high performance gel filtration chromatography.

1996 ◽  
Vol 45 (1) ◽  
pp. 103-106 ◽  
Author(s):  
Takashi KITAMURA ◽  
Seiji ITO ◽  
Yoshio KATO ◽  
Keiko SASAMOTO ◽  
Mitsuyo OKAZAKI
Keyword(s):  
High Performance ◽  
Gel Filtration ◽  
Serum Lipoproteins ◽  
Gel Filtration Chromatography

scholarly journals Structural and Functional Conversion of Molecular Chaperone ClpB from the Gram-Positive Halophilic Lactic Acid Bacterium Tetragenococcus halophilus Mediated by ATP and Stress

2006 ◽  
Vol 188 (23) ◽  
pp. 8070-8078 ◽  
Author(s):  
Shinya Sugimoto ◽  
Hiroyuki Yoshida ◽  
Yoshimitsu Mizunoe ◽  
Keigo Tsuruno ◽  
Jiro Nakayama ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacterium ◽  
Molecular Chaperone ◽  
Thermal Inactivation ◽  
Gel Filtration ◽  
Ring Structure ◽  
Stress Conditions ◽  
Gel Filtration Chromatography ◽  
Gram Positive ◽  
Tetragenococcus Halophilus

ABSTRACT In this study, we report the purification, initial structural characterization, and functional analysis of the molecular chaperone ClpB from the gram-positive, halophilic lactic acid bacterium Tetragenococcus halophilus. A recombinant T. halophilus ClpB (ClpB Tha ) was overexpressed in Escherichia coli and purified by affinity chromatography, hydroxyapatite chromatography, and gel filtration chromatography. As demonstrated by gel filtration chromatography, chemical cross-linking with glutaraldehyde, and electron microscopy, ClpB Tha forms a homohexameric single-ring structure in the presence of ATP under nonstress conditions. However, under stress conditions, such as high-temperature (>45°C) and high-salt concentrations (>1 M KCl), it dissociated into dimers and monomers, regardless of the presence of ATP. The hexameric ClpB Tha reactivated heat-aggregated proteins dependent upon the DnaK system from T. halophilus (KJE Tha ) and ATP. Interestingly, the mixture of dimer and monomer ClpB Tha , which was formed under stress conditions, protected substrate proteins from thermal inactivation and aggregation in a manner similar to those of general molecular chaperones. From these results, we hypothesize that ClpB Tha forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a disaggregating chaperone in cooperation with KJE Tha and ATP under poststress conditions.

Isolation and Structural Characterization of Antioxidant Peptides from Degreased Apricot Seed Kernels

2018 ◽  
Vol 101 (5) ◽  
pp. 1661-1663 ◽  
Author(s):  
Haisheng Zhang ◽  
Jing Xue ◽  
Huanxia Zhao ◽  
Xinshuai Zhao ◽  
Huanhuan Xue ◽  
...  
Keyword(s):  
Amino Acid ◽  
Antioxidant Activities ◽  
Gel Filtration ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Seed Kernel ◽  
Antioxidant Peptides ◽  
Food Preservatives ◽  
Isolation And Purification ◽  
Rp Hplc

Abstract Background: The composition and sequence of amino acids have a prominent influence on the antioxidant activities of peptides. Objective: A series of isolation and purification experiments was conducted to explore the amino acid sequence of antioxidant peptides, which led to its antioxidation causes. Methods: The degreased apricot seed kernels were hydrolyzed by compound proteases of alkaline protease and flavor protease (3:2, u/u) to prepare apricot seed kernel hydrolysates (ASKH). ASKH were separated into ASKH-A and ASKH-B by dialysis bag. ASKH-B (MW < 3.5 kDa) was further separated into fractions by Sephadex G-25 and G-15 gel-filtration chromatography. Reversed-phase HPLC (RP-HPLC) was performed to separate fraction B4b into two antioxidant peptides (peptide B4b-4 and B4b-6). Results: The amino acid sequences were Val-Leu-Tyr-Ile-Trp and Ser-Val-Pro-Tyr-Glu, respectively. Conclusions: The results suggested that ASKH antioxidant peptides may have potential utility as healthy ingredients and as food preservatives due to their antioxidant activity. Highlights: Materials with regional characteristics were selected to explore, and hydrolysates were identified by RP-HPLC and matrix-assisted laser desorption ionization-time-of-flight-MS to obtain amino acid sequences.

Sign in / Sign up

Export Citation Format

Share Document