What question did this study set out to answer?

The research aims to explore the ACE-I activity of peptides derived from germinated lamtoro gung seeds.

January 10, 2026Preventive Nutrition and Food Science0 citationsOpen Access

Investigation of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Germinated Lamtoro Gung Using In Vitro and In Silico Approaches

AFAprilia Fitriani Aprilia FitrianiUniversitas Ahmad Dahlan RIRetno IndratiUniversitas Gadjah Mada YMYustinus MarsonoUniversitas Gadjah Mada

Key Result

Germination for 48 hours led to a peak ACE-I activity of 70.62% in lamtoro gung seeds, suggesting potential for functional antihypertensive food substances.

Key Points

The research aims to explore the ACE-I activity of peptides derived from germinated lamtoro gung seeds.
Germinated lamtoro gung seeds were analyzed at various intervals over 120 hours.
In vitro and in silico methods were utilized to assess peptide characteristics and interactions.
Liquid chromatography-mass spectrometry characterized peptide sequences.
Molecular docking simulations evaluated interactions of selected peptides with ACE.
The sample germinated for 48 hours exhibited the highest ACE-I activity at 70.62%.
Forty peptide sequences were identified within the 1-3.5 kDa molecular weight range with ACE-I activity.
Two specific peptide sequences, VEIKVTVK and KNEVAINELK, showed strong potential to interact with ACE.

Structured PICO

Do peptides derived from germinated lamtoro gung seeds inhibit ACE activity in vitro?

Population

In vitro and in silico models using lamtoro gung seeds and Angiotensin I-converting enzyme (ACE)

Intervention

Peptides extracted from lamtoro gung seeds germinated for 48 hours

Comparator

Captopril (positive control) and non-germinated/blank controls

Outcome

Angiotensin I-converting enzyme inhibitory (ACE-I) activitysurrogate

Peptides derived from germinated lamtoro gung seeds demonstrate significant in vitro ACE inhibitory activity, highlighting their potential as functional food ingredients for hypertension management.

Main Result

Absolute Event Rate: 0% vs 0%

Abstract

Angiotensin I-converting enzyme inhibitory (ACE-I) peptides derived from food sources have been extensively researched. These peptides can be derived during the germination process. This study investigated the ACE-I activity of lamtoro gung seeds during the germination process. This work used in vitro and in silico methodologies to address the research issues. Lamtoro gung seeds were germinated for 120 h. The sprouts exhibiting the highest ACE-I activity were assessed for low-molecular-weight (LMW) peptide content and molecular distribution. Subsequently, the peptide sequence of the peptide fraction with a 1－3.5 kDa molecular weight range was characterized using liquid chromatography-mass spectrometry. The peptide sequence with the highest support vector machine score was chosen for molecular docking simulation to examine the interaction between peptides and ACE. The sample germinated for 48 h had the highest ACE-I activity (70.62%) as confirmed by the increased amount of LMW peptides (<1 and 1－3.5 kDa). Forty peptide sequences with ACE-I activity were identified in the <1 to 3.5 kDa fractions. Two peptide sequences (VEIKVTVK and KNEVAINELK) were predicted to interact with the active site of ACE according to molecular docking simulations. This research suggests that germination could serve as an alternative method for producing functional food substances that act as antihypertensive agents.

Ask AI

Helpful

Bookmark

View Full Paper