Valorization of an Abundant Slaughterhouse By-product as a Source of Highly Technofunctional and Antioxidant Protein Hydrolysates

被引:16
作者
da Silva Bambirra Alves, Fillemon Edillyn [1 ]
Carpine, Danielle [1 ]
Teixeira, Gerson Lopes [2 ]
Goedert, Ana Caroline [3 ]
de Paula Scheer, Agnes [1 ]
Ribani, Rosemary Hoffmann [1 ]
机构
[1] Univ Fed Parana, Food Engn Grad Program, Polytech Ctr, BR-82590300 Curitiba, Parana, Brazil
[2] Univ Fed Santa Catarina, Dept Food Sci & Technol, Campus Florianopolis, BR-88034001 Florianopolis, SC, Brazil
[3] Univ Fed Parana, Dept Biochem & Mol Biol, Polytech Ctr, BR-81531980 Curitiba, Parana, Brazil
关键词
Chicken blood meal; Peptides; Degree of hydrolysis; Emulsifying properties; Foaming properties; Antioxidant activity; FUNCTIONAL-PROPERTIES; BITTERNESS PROPERTIES; SECONDARY STRUCTURE; WHEY-PROTEIN; ISOLATE; FOOD; BLOOD; PORCINE; INHIBITION; PEPTIDES;
D O I
10.1007/s12649-020-00985-8
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
Purpose Chicken blood meal (CBM) is a slaughterhouse by-product of great environmental concern, rich in protein and iron, mainly used as animal feed and fertilizer. In this work, the valorization of CBM as a source of protein hydrolysates (CBMH) is proposed. Methods The hydrolysis reaction conditions were assessed using a Doehlert experimental design. Samples of CBMH were thus prepared at optimal conditions: T = 54 degrees C, pH 8.5 and enzyme-to-substrate ratio (E/S) = 6.5% with different reaction durations in order to study the impact of the degree of hydrolysis (DH) on the properties of the product. The characteristics studied in the hydrolysates were among others: chemical structure, technofunctional properties [compared to those from soy protein isolate (SPI)] and antioxidant activity. Results CBMH samples displayed MW < 14.4 kDa, increasing heme content correlated with their color parameters, formation of hygroscope aggregates and enhanced thermal stability. UV-spectroscopy, infrared spectroscopy and circular dichroism confirmed the conformational changes in CBMH to be dependent on the DH. Compared to CBM, CBMH had improved oil holding capacity that decreased with the DH. CBMH foams exhibited better behavior at neutral pH than those from SPI. Moreover, CBMH emulsions displayed lower emulsifying activity and higher but decreasing emulsifying stability. CBMH samples displayed antioxidant activity (FRAP, DPPH and ABTS), whereas only the FRAP values suffered a negative impact due to the extended hydrolysis. Conclusions The results suggest that the valorization of CBM can be achieved via hydrolysis, resulting in potential ingredients for the food, cosmetic and pharmaceutical industries. Graphic
引用
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页码:263 / 279
页数:17
相关论文
共 93 条
[1]  
Adler-Nissen, 1986, ENZYMIC HYDROLYSIS F
[2]   QUANTITATIVE STUDIES OF THE STRUCTURE OF PROTEINS IN SOLUTION BY FOURIER-TRANSFORM INFRARED-SPECTROSCOPY [J].
ARRONDO, JLR ;
MUGA, A ;
CASTRESANA, J ;
GONI, FM .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1993, 59 (01) :23-56
[3]  
*ASS OFF AGR CHEM, 1990, AOAC OFF METH AN
[4]   Production of bioactive peptide hydrolysates from deer, sheep, pig and cattle red blood cell fractions using plant and fungal protease preparations [J].
Bah, Clara S. F. ;
Carne, Alan ;
McConnell, Michelle A. ;
Mros, Sonya ;
Bekhit, Alaa El-Din A. .
FOOD CHEMISTRY, 2016, 202 :458-466
[5]   Slaughterhouse Blood: An Emerging Source of Bioactive Compounds [J].
Bah, Clara S. F. ;
Bekhit, Alaa El-Din A. ;
Carne, Alan ;
McConnell, Michelle A. .
COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY, 2013, 12 (03) :314-331
[6]  
Barr Ian, 2015, Bio Protoc, V5
[7]   Feather Protein Hydrolysates: A Study of Physicochemical, Functional Properties and Antioxidant Activity [J].
Ben Hamad Bouhamed, Sana ;
Krichen, Fatma ;
Kechaou, Nabil .
WASTE AND BIOMASS VALORIZATION, 2020, 11 (01) :51-62
[8]   The ferric reducing ability of plasma (FRAP) as a measure of ''antioxidant power'': The FRAP assay [J].
Benzie, IFF ;
Strain, JJ .
ANALYTICAL BIOCHEMISTRY, 1996, 239 (01) :70-76
[9]   SIMULTANEOUS DETERMINATION OF HEMES-A, HEMES-B, AND HEMES-C FROM PYRIDINE HEMOCHROME SPECTRA [J].
BERRY, EA ;
TRUMPOWER, BL .
ANALYTICAL BIOCHEMISTRY, 1987, 161 (01) :1-15
[10]  
Böcker U, 2017, ANALYST, V142, P2812, DOI [10.1039/c7an00488e, 10.1039/C7AN00488E]