Bamboo Leaf Protein Concentrate: Wet Fractionation, Protein Secondary Structure, Digestibility, Trypsin Inhibition

The protein that is separated from the fibrous leafy portions of plant materials is called leaf protein concentrate (LPC). In this study, fermentation of green juice of fresh bamboo leaves resulted in LPC with the highest crude protein content. Osborne fractionation revealed that nearly 60% of soluble proteins in bamboo LPC are alkali-soluble (glutelin). In all cases of precipitation methods employed, bamboo LPCs had the highest percentage of glutelins in them, followed by prolamins, albumins, and globulins. Protein in vitro digestibility showed a positive correlation with α-helix:β-sheets ratio of bamboo LPCs. Overall protein in vitro digestibility study indicated that acid-precipitated LPC was most digestible. Trypsin inhibition activity (TIA)% was evaluated through the Kunitz method and FTIR. Results revealed that acid-precipitated bamboo LPC had the lowest degree of TIA%. A higher degree of TIA% reduction was achieved at 121 °C than at 100 °C. In the case of adsorption by activated carbon, activation energy was observed to decrease with increasing initial TIA% in bamboo LPCs. Correlation analysis of various quality attributes of bamboo LPC obtained from different precipitation methods revealed the importance of Osborne fractionation in the initial selection procedure of leaf sources and concentration methods.

Authors

Institutions

Publication Details

Journal
ACS Food Science & Technology
Published
2025-04-15
DOI
https://doi.org/10.1021/acsfoodscitech.4c01010
Citations
1
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
1.16
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Bamboo Leaf Protein Concentrate: Wet Fractionation, Protein Secondary Structure, Digestibility, Trypsin Inhibition

Debanjana Biswas, Soumya Ranjan Purohit
1 citations
ACS Food Science & Technology
Proteins in Food Systems
1.16
article

Bamboo Leaf Protein Concentrate: Wet Fractionation, Protein Secondary Structure, Digestibility, Trypsin Inhibition

Debanjana Biswas, Soumya Ranjan Purohit
article en
1 citations

Abstract

The protein that is separated from the fibrous leafy portions of plant materials is called leaf protein concentrate (LPC). In this study, fermentation of green juice of fresh bamboo leaves resulted in LPC with the highest crude protein content. Osborne fractionation revealed that nearly 60% of soluble proteins in bamboo LPC are alkali-soluble (glutelin). In all cases of precipitation methods employed, bamboo LPCs had the highest percentage of glutelins in them, followed by prolamins, albumins, and globulins. Protein in vitro digestibility showed a positive correlation with α-helix:β-sheets ratio of bamboo LPCs. Overall protein in vitro digestibility study indicated that acid-precipitated LPC was most digestible. Trypsin inhibition activity (TIA)% was evaluated through the Kunitz method and FTIR. Results revealed that acid-precipitated bamboo LPC had the lowest degree of TIA%. A higher degree of TIA% reduction was achieved at 121 °C than at 100 °C. In the case of adsorption by activated carbon, activation energy was observed to decrease with increasing initial TIA% in bamboo LPCs. Correlation analysis of various quality attributes of bamboo LPC obtained from different precipitation methods revealed the importance of Osborne fractionation in the initial selection procedure of leaf sources and concentration methods.

ACS Food Science & TechnologyVol. 5(5)
Tezpur University (IN)
Zero hunger
Openalex Percentile: Top 23%
Proteins in Food Systems
1.16
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.