Optimization of trypsin-assisted extraction, physico-chemical characterization, nutritional qualities and functionalities of palm kernel cake protein

K. L. Chee, H. K. Ling, Mohd. Khan Ayob

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24 Citations (Scopus)

Abstract

The extraction of palm kernel cake protein (PKCP) was enhanced by trypsin-assisted assay. From the Response Surface Methodology (RSM) generated model, the optimum conditions were using trypsin at concentration 1.36g/100g, reacted on palm kernel cake (PKC) slurry (1.1g/100mL) at 50°C and pH 9.5. The trypsin extracted protein yield (61.99±0.74g/100g) was significantly (P<0.05) higher than the alkaline (pH 9.5) method (10.21±0.24g/100g). Surface hydrophobicity of PKCP (159.36) was significantly (P<0.05) higher than soy protein isolate (SPI) (51.51). PKCP had a lower denatured temperature (66.88°C) than SPI (101.41°C). The electrophoretograms of PKCP showed 3 bands at 2.20, 3.51 and 4.28kDa, compared to SPI which had 22 bands with molecular weight ranging from 2.00 to 82.79kDa. Except lysine, the essential amino acids of PKCP met the suggested requirements of FAO/WHO for 2-5 year old infants. The in-vitro digestibility, essential amino acids/total amino acids (E/T) value, biological value and computed-protein efficiency ratio (C-PER) value for PKCP were significantly (P<0.05) higher than that of SPI. PKCP also showed better solubility (30.12-97.79 vs. 9.15-69.78g/100g) emulsifying activity (143.25 vs. 32.57m 2/g); but lower emulsifying stability (37.83 vs. 43.08%), foaming capacity (22.5 vs. 100.0 ml/100ml) and foam stability (3.70 vs. 19.20ml) than the SPI.

Original languageEnglish
Pages (from-to)419-427
Number of pages9
JournalLWT - Food Science and Technology
Volume46
Issue number2
DOIs
Publication statusPublished - May 2012

Fingerprint

palm kernel cake
Nutritive Value
Trypsin
trypsin
nutritive value
Soybean Proteins
soy protein isolate
Proteins
proteins
Essential Amino Acids
emulsifying
essential amino acids
Erythrocyte Anion Exchange Protein 1
foaming capacity
in vitro digestibility
protein efficiency ratio
foams
hydrophobicity
response surface methodology
Hydrophobic and Hydrophilic Interactions

Keywords

  • Amino acid composition
  • Emulsifying properties
  • Palm kernel cake protein extraction
  • Response surface methodology
  • Trypsin

ASJC Scopus subject areas

  • Food Science

Cite this

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title = "Optimization of trypsin-assisted extraction, physico-chemical characterization, nutritional qualities and functionalities of palm kernel cake protein",
abstract = "The extraction of palm kernel cake protein (PKCP) was enhanced by trypsin-assisted assay. From the Response Surface Methodology (RSM) generated model, the optimum conditions were using trypsin at concentration 1.36g/100g, reacted on palm kernel cake (PKC) slurry (1.1g/100mL) at 50°C and pH 9.5. The trypsin extracted protein yield (61.99±0.74g/100g) was significantly (P<0.05) higher than the alkaline (pH 9.5) method (10.21±0.24g/100g). Surface hydrophobicity of PKCP (159.36) was significantly (P<0.05) higher than soy protein isolate (SPI) (51.51). PKCP had a lower denatured temperature (66.88°C) than SPI (101.41°C). The electrophoretograms of PKCP showed 3 bands at 2.20, 3.51 and 4.28kDa, compared to SPI which had 22 bands with molecular weight ranging from 2.00 to 82.79kDa. Except lysine, the essential amino acids of PKCP met the suggested requirements of FAO/WHO for 2-5 year old infants. The in-vitro digestibility, essential amino acids/total amino acids (E/T) value, biological value and computed-protein efficiency ratio (C-PER) value for PKCP were significantly (P<0.05) higher than that of SPI. PKCP also showed better solubility (30.12-97.79 vs. 9.15-69.78g/100g) emulsifying activity (143.25 vs. 32.57m 2/g); but lower emulsifying stability (37.83 vs. 43.08{\%}), foaming capacity (22.5 vs. 100.0 ml/100ml) and foam stability (3.70 vs. 19.20ml) than the SPI.",
keywords = "Amino acid composition, Emulsifying properties, Palm kernel cake protein extraction, Response surface methodology, Trypsin",
author = "Chee, {K. L.} and Ling, {H. K.} and Ayob, {Mohd. Khan}",
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AU - Chee, K. L.

AU - Ling, H. K.

AU - Ayob, Mohd. Khan

PY - 2012/5

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N2 - The extraction of palm kernel cake protein (PKCP) was enhanced by trypsin-assisted assay. From the Response Surface Methodology (RSM) generated model, the optimum conditions were using trypsin at concentration 1.36g/100g, reacted on palm kernel cake (PKC) slurry (1.1g/100mL) at 50°C and pH 9.5. The trypsin extracted protein yield (61.99±0.74g/100g) was significantly (P<0.05) higher than the alkaline (pH 9.5) method (10.21±0.24g/100g). Surface hydrophobicity of PKCP (159.36) was significantly (P<0.05) higher than soy protein isolate (SPI) (51.51). PKCP had a lower denatured temperature (66.88°C) than SPI (101.41°C). The electrophoretograms of PKCP showed 3 bands at 2.20, 3.51 and 4.28kDa, compared to SPI which had 22 bands with molecular weight ranging from 2.00 to 82.79kDa. Except lysine, the essential amino acids of PKCP met the suggested requirements of FAO/WHO for 2-5 year old infants. The in-vitro digestibility, essential amino acids/total amino acids (E/T) value, biological value and computed-protein efficiency ratio (C-PER) value for PKCP were significantly (P<0.05) higher than that of SPI. PKCP also showed better solubility (30.12-97.79 vs. 9.15-69.78g/100g) emulsifying activity (143.25 vs. 32.57m 2/g); but lower emulsifying stability (37.83 vs. 43.08%), foaming capacity (22.5 vs. 100.0 ml/100ml) and foam stability (3.70 vs. 19.20ml) than the SPI.

AB - The extraction of palm kernel cake protein (PKCP) was enhanced by trypsin-assisted assay. From the Response Surface Methodology (RSM) generated model, the optimum conditions were using trypsin at concentration 1.36g/100g, reacted on palm kernel cake (PKC) slurry (1.1g/100mL) at 50°C and pH 9.5. The trypsin extracted protein yield (61.99±0.74g/100g) was significantly (P<0.05) higher than the alkaline (pH 9.5) method (10.21±0.24g/100g). Surface hydrophobicity of PKCP (159.36) was significantly (P<0.05) higher than soy protein isolate (SPI) (51.51). PKCP had a lower denatured temperature (66.88°C) than SPI (101.41°C). The electrophoretograms of PKCP showed 3 bands at 2.20, 3.51 and 4.28kDa, compared to SPI which had 22 bands with molecular weight ranging from 2.00 to 82.79kDa. Except lysine, the essential amino acids of PKCP met the suggested requirements of FAO/WHO for 2-5 year old infants. The in-vitro digestibility, essential amino acids/total amino acids (E/T) value, biological value and computed-protein efficiency ratio (C-PER) value for PKCP were significantly (P<0.05) higher than that of SPI. PKCP also showed better solubility (30.12-97.79 vs. 9.15-69.78g/100g) emulsifying activity (143.25 vs. 32.57m 2/g); but lower emulsifying stability (37.83 vs. 43.08%), foaming capacity (22.5 vs. 100.0 ml/100ml) and foam stability (3.70 vs. 19.20ml) than the SPI.

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KW - Response surface methodology

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