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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/52972

Title: Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana.
Authors: Yu‐Wei Chang
Encarnacion Emilia S. Yap
Jose P. Peralta
Lhumen A. Tejano
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: angiotensin‐converting enzyme inhibitory
antibacterial activity
Chlorella sorokiniana
Date: 2019-07
Issue Date: 2020-06-15T08:50:42Z
Publisher: FOOD SCIENCE & TECHNOLOGY
Abstract: Abstract:
Chlorella sorokiniana protein isolates were enzymatically hydrolyzed using pepsin, bromelain, and thermolysin, with their molecular characteristics and bioactivities determined. Thermolysin hydrolysates exhibited the highest degree of hydrolysis (18.08% ± 1.13%). The sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) results showed that peptides with molecular weights <10 kDa were found in the hydrolysates compared to the protein isolates. Bioactivity assays revealed that pepsin peptide fraction <5 kDa showed the highest angiotensin‐converting enzyme (ACE)‐inhibitory (34.29% ± 3.45%) and DPPH radical scavenging activities (48.86% ± 1.95%), while pepsin peptide fraction <10 kDa demonstrated the highest reducing power with 0.2101% ± 0.02% absorbance. Moreover, antibacterial assessment revealed that pepsin hydrolysate and peptide fractions displayed inhibition to the test microorganisms. Overall, the present findings suggest that C. sorokiniana protein hydrolysates can be valuable bio‐ingredients with pharmaceutical and nutraceutical application potentials.
Relation: 7(7) pp 2381-2390
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/52972
Appears in Collections:[食品科學系] 期刊論文

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