Aloe vera leaves potential as a new source of transglutaminase

Transglutaminase is an enzyme that catalyzes cross-linking reactions between primary protein chains. This activity can be applied to improve the texture quality of protein-based food products, such as meatballs, and surimi sausage. Elasticity is an important parameter for consumers when choosing these food products. Currently, many chemical compounds of phosphate have been used to increase the elasticity of food products. Therefore, this study aimed to use plant-derived transglutaminase as a gelling agent for food products to replace chemicals. The experiment was carried out by extracting transglutaminase from aloe vera leaves for characterization. The parameters characterized include transglutaminase activity, optimum temperature and pH, molecular weight, as well as inhibiting and activating compounds. The results showed that aloe vera leaves extract had high transglutaminase activity (0.47 U.mg-1), optimum temperature of 40-50°C, pH 5-7, molecular weight of 70-75 kDa, strongly inhibited by Zn2+ ions, and activated in the presence of dithiothreitol (DTT). The high activity shows that aloe vera leaves can be applied as a gelling agent in food products.

Authors

Institutions

Publication Details

Journal
AGROINTEK
Published
2025-01-22
DOI
https://doi.org/10.21107/agrointek.v19i1.27877
Citations
1
Primary Topic
Phytochemistry and biological activity of medicinal plants
Type
article
Field-Weighted Citation Impact
1.75

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Aloe vera leaves potential as a new source of transglutaminase

Wahyu Prihanta, Cahyo Indarto, Supriyanto Supriyanto, Dang Ngoc Hung
1 citations
AGROINTEK
Phytochemistry and biological activity of medicinal plants
1.75
article

Aloe vera leaves potential as a new source of transglutaminase

Wahyu Prihanta, Cahyo Indarto, Supriyanto Supriyanto, Dang Ngoc Hung
article en
1 citations

Abstract

Transglutaminase is an enzyme that catalyzes cross-linking reactions between primary protein chains. This activity can be applied to improve the texture quality of protein-based food products, such as meatballs, and surimi sausage. Elasticity is an important parameter for consumers when choosing these food products. Currently, many chemical compounds of phosphate have been used to increase the elasticity of food products. Therefore, this study aimed to use plant-derived transglutaminase as a gelling agent for food products to replace chemicals. The experiment was carried out by extracting transglutaminase from aloe vera leaves for characterization. The parameters characterized include transglutaminase activity, optimum temperature and pH, molecular weight, as well as inhibiting and activating compounds. The results showed that aloe vera leaves extract had high transglutaminase activity (0.47 U.mg-1), optimum temperature of 40-50°C, pH 5-7, molecular weight of 70-75 kDa, strongly inhibited by Zn2+ ions, and activated in the presence of dithiothreitol (DTT). The high activity shows that aloe vera leaves can be applied as a gelling agent in food products.

AGROINTEKVol. 19(1)
Universitas Trunodjoyo Madura (ID), Universitas Muhammadiyah Malang (ID), Thai Nguyen University of Agriculture and Forestry (VN)
Kementerian Pendidikan, Kebudayaan, Riset, dan Teknologi, Direktorat Jenderal Pendidikan Tinggi
Openalex Percentile: Top 17%
Phytochemistry and biological activity of medicinal plants
1.75
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Aloe vera leaves potential as a new source of transglutaminase — Wahyu Prihanta, Cahyo Indarto, et al. · AGROINTEK (2025) | TGRS Research Map | TGRS