Physicochemical and functional properties of Alcalase‐extracted protein hydrolysate from oil palm leaves

Hau, Eng Huan; Teh, Soek Sin; Yeo, Siok Koon; Mah, Siau Hui

doi:10.1002/jsfa.11350

Cited by 5 publications

(2 citation statements)

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“…The protein content in the supernatant was measured using the Lowry method, and the total protein content was measured using the Kjeldahl method. The solubility was calculated according to 21

Solubility (%) = \frac{P_{1}}{P_{0}} \times 100

where P 1 (mg g −1 ) is the supernatant protein content and P 0 (mg g −1 ) is the total protein content.…”

Section: Methodsmentioning

confidence: 99%

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Structure, physicochemical properties, and biological activities of protein hydrolysates from Zanthoxylum seed

Dong,

Li,

Sun

et al. 2023

J Sci Food Agric

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BACKGROUNDZanthoxylum seed, as a low‐cost and easily accessible plant protein resource, has good potential in the food industry. But protein and its hydrolysates from Zanthoxylum seed are underutilized due to the dearth of studies on them. This study aimed to investigate the structure and physicochemical and biological activities of Zanthoxylum seed protein (ZSP) hydrolysates prepared using Protamex®, Alcalase®, Neutrase®, trypsin, or pepsin.RESULTSHydrolysis using each of the five enzymes diminished average particle size and molecular weight of ZSP but increased random coil content. ZSP hydrolysate prepared using pepsin had the highest degree of hydrolysis (24.07%) and the smallest molecular weight (<13 kDa) and average particle size (129.80 nm) with the highest solubility (98.9%). In contrast, ZSP hydrolysate prepared using Alcalase had the highest surface hydrophobicity and foaming capacity (88.89%), as well as the lowest foam stability (45.00%). Moreover, ZSP hydrolysate prepared using Alcalase exhibited the best hydroxyl‐radical scavenging (half maximal inhibitory concentration (IC50) 1.94 mg mL−1) and ferrous‐ion chelating (IC50 0.61 mg mL−1) activities. Additionally, ZSP hydrolysate prepared using pepsin displayed the highest angiotensin‐converting enzyme inhibition activity (IC50 0.54 mg mL−1).CONCLUSIONThese data showed that enzyme hydrolysis improved the physicochemical properties of ZSP, and enzymatic hydrolysates of ZSP exhibited significant biological activity. These results provided validation for application of ZSP enzymatic hydrolysates as antioxidants and antihypertensive agents in the food or medicinal industries. © 2023 Society of Chemical Industry.

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“…The protein content in the supernatant was measured using the Lowry method, and the total protein content was measured using the Kjeldahl method. The solubility was calculated according to 21

Solubility (%) = \frac{P_{1}}{P_{0}} \times 100

where P 1 (mg g −1 ) is the supernatant protein content and P 0 (mg g −1 ) is the total protein content.…”

Section: Methodsmentioning

confidence: 99%

“…The protein content in the supernatant was measured using the Lowry method, and the total protein content was measured using the Kjeldahl method. The solubility was calculated according to 21 Solubility % ð Þ=…”

Section: Solubilitymentioning

confidence: 99%