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     Research Journal of Applied Sciences, Engineering and Technology


Synthesis of Protein Hydrolysate from the Prepupae of Hermetia illucens using a Papain Enzymes

1, 2Rini Triani, 1Rika Alfianny, 1Robert Manurung and 1Muhammad Yusuf Abduh
1School of Life Sciences and Technology, Institut Teknologi Bandung, Jalan Ganesha 10, Bandung 40132, Indonesia
2Faculty of Engineering Pasundan University, Jalan Dr. Setiabudhhi No. 193, Bandung 40153, Indonesia
Research Journal of Applied Sciences, Engineering and Technology  2021  1:12-19
http://dx.doi.org/10.19026/rjaset.18.6059  |  © The Author(s) 2021
Received: April 14, 2020  |  Accepted: May 8, 2020  |  Published: March 25, 2021

Abstract

The aim of this study was to determine optimum enzyme concentration and hydrolysis time needed to hydrolyze black soldier fly prepupae into a protein hydrolysate. The prepupae were homogenized with aquadest and papain enzyme (0-9% on a weight basis) at pH 7 for 24-72 h at 55°C. At optimum conditions (enzyme concentration of 6% on a weight basis and hydrolysis time of 24 h), the yield of protein hydrolysate was 31% on a dry weight basis. The protein content increased from 39.7 to 61% (dry weight basis) whereas the lipid content in the protein hydrolysate decreased from 30.3 to 0.5% (dry weight basis). Hydrolysis of the prepupae with a papain enzyme increased the amino acid content from 15.4 to 47.1% on a weight basis. The black soldier fly prepupae contains 15 detectable amino acids primarily consists of glutamic acid (10.7%), alanine (10.7%), leucine (10%) and valine (9%). After hydrolysis with a papain enzyme, the composition of the amino acid changed and primarily consists of glutamic acid (17.3%), tyrosine (9.4%), leucine (9.4%) and alanine (8.9%). The protein hydrolysate may find application as a supplement for feed and food for a better absorption of nutrients in animal intestine.

Keywords:

Amino acid, black soldier fly prepupae, enzymatic hydrolysis, papain, protein hydrolysate,


References


Competing interests

The authors have no competing interests.

Open Access Policy

This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

Copyright

The authors have no competing interests.

ISSN (Online):  2040-7467
ISSN (Print):   2040-7459
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