An integrated strategy for the effective production of bristle protein hydrolysate by the keratinolytic filamentous bacterium Amycolatopsis keratiniphila D2

Francesco Cristino Falco*, Roall Espersen, Birte Svensson, Krist V. Gernaey, Anna Eliasson Lantz

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

In a conventional microorganism-mediated biological process for degradation of keratinous waste material the production of keratin-specific proteases (i.e., keratinases) and the hydrolysis of keratin-rich residual biomass both take place during the same stage of the bioprocess and, as a consequence, occur simultaneously under suboptimal conditions. In the present study the keratinolytic actinomycete Amycolatopsis keratiniphila D2 was successfully employed to biodegrade thermally pretreated porcine bristles at high solids loading (16% w/v) via a novel cultivation methodology. Indeed, the two-stage submerged fermentation process developed in this work enabled to efficiently recover, in a single unit operation, about 73% of the protein material contained in the keratinous biowaste structure, resulting in an overall accumulation of 89.3 g·L−1 protein-rich hydrolysate and a productivity of 427 mg crude soluble proteins per litre per hour. The obtained protein hydrolysate powder displayed a 2.2-fold increase in its in vitro pepsin digestibility (95%) with respect to the non-hydrolysed pretreated substrate (43%). In addition, the chromatogram obtained by size-exclusion chromatography analysis of the final product indicated that, among the identified fractions, those consisting of small peptides and free amino acids were the most abundantly present inside the analysed sample. Given these facts it is possible to conclude that the soluble proteins, peptides and free amino acids recovered through the newly designed two-stage bioextraction process could represent a viable alternative source of protein in animal feed formulation.
Original languageEnglish
JournalWaste Management
Volume89
Pages (from-to)94-102
ISSN0956-053X
DOIs
Publication statusPublished - 2019

Keywords

  • Pretreated pig bristle
  • Amycolatopsis keratiniphila
  • Two-stage bioprocess
  • Keratin biodegradation
  • Keratinolytic protease
  • Bristle protein hydrolysate

Cite this

@article{43c17c91bf8748c1b9c05e07b942a915,
title = "An integrated strategy for the effective production of bristle protein hydrolysate by the keratinolytic filamentous bacterium Amycolatopsis keratiniphila D2",
abstract = "In a conventional microorganism-mediated biological process for degradation of keratinous waste material the production of keratin-specific proteases (i.e., keratinases) and the hydrolysis of keratin-rich residual biomass both take place during the same stage of the bioprocess and, as a consequence, occur simultaneously under suboptimal conditions. In the present study the keratinolytic actinomycete Amycolatopsis keratiniphila D2 was successfully employed to biodegrade thermally pretreated porcine bristles at high solids loading (16{\%} w/v) via a novel cultivation methodology. Indeed, the two-stage submerged fermentation process developed in this work enabled to efficiently recover, in a single unit operation, about 73{\%} of the protein material contained in the keratinous biowaste structure, resulting in an overall accumulation of 89.3 g·L−1 protein-rich hydrolysate and a productivity of 427 mg crude soluble proteins per litre per hour. The obtained protein hydrolysate powder displayed a 2.2-fold increase in its in vitro pepsin digestibility (95{\%}) with respect to the non-hydrolysed pretreated substrate (43{\%}). In addition, the chromatogram obtained by size-exclusion chromatography analysis of the final product indicated that, among the identified fractions, those consisting of small peptides and free amino acids were the most abundantly present inside the analysed sample. Given these facts it is possible to conclude that the soluble proteins, peptides and free amino acids recovered through the newly designed two-stage bioextraction process could represent a viable alternative source of protein in animal feed formulation.",
keywords = "Pretreated pig bristle, Amycolatopsis keratiniphila, Two-stage bioprocess, Keratin biodegradation, Keratinolytic protease, Bristle protein hydrolysate",
author = "Falco, {Francesco Cristino} and Roall Espersen and Birte Svensson and Gernaey, {Krist V.} and {Eliasson Lantz}, Anna",
year = "2019",
doi = "10.1016/j.wasman.2019.03.067",
language = "English",
volume = "89",
pages = "94--102",
journal = "Waste Management",
issn = "0956-053X",
publisher = "Pergamon Press",

}

An integrated strategy for the effective production of bristle protein hydrolysate by the keratinolytic filamentous bacterium Amycolatopsis keratiniphila D2. / Falco, Francesco Cristino; Espersen, Roall; Svensson, Birte; Gernaey, Krist V.; Eliasson Lantz, Anna.

In: Waste Management, Vol. 89, 2019, p. 94-102.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - An integrated strategy for the effective production of bristle protein hydrolysate by the keratinolytic filamentous bacterium Amycolatopsis keratiniphila D2

AU - Falco, Francesco Cristino

AU - Espersen, Roall

AU - Svensson, Birte

AU - Gernaey, Krist V.

AU - Eliasson Lantz, Anna

PY - 2019

Y1 - 2019

N2 - In a conventional microorganism-mediated biological process for degradation of keratinous waste material the production of keratin-specific proteases (i.e., keratinases) and the hydrolysis of keratin-rich residual biomass both take place during the same stage of the bioprocess and, as a consequence, occur simultaneously under suboptimal conditions. In the present study the keratinolytic actinomycete Amycolatopsis keratiniphila D2 was successfully employed to biodegrade thermally pretreated porcine bristles at high solids loading (16% w/v) via a novel cultivation methodology. Indeed, the two-stage submerged fermentation process developed in this work enabled to efficiently recover, in a single unit operation, about 73% of the protein material contained in the keratinous biowaste structure, resulting in an overall accumulation of 89.3 g·L−1 protein-rich hydrolysate and a productivity of 427 mg crude soluble proteins per litre per hour. The obtained protein hydrolysate powder displayed a 2.2-fold increase in its in vitro pepsin digestibility (95%) with respect to the non-hydrolysed pretreated substrate (43%). In addition, the chromatogram obtained by size-exclusion chromatography analysis of the final product indicated that, among the identified fractions, those consisting of small peptides and free amino acids were the most abundantly present inside the analysed sample. Given these facts it is possible to conclude that the soluble proteins, peptides and free amino acids recovered through the newly designed two-stage bioextraction process could represent a viable alternative source of protein in animal feed formulation.

AB - In a conventional microorganism-mediated biological process for degradation of keratinous waste material the production of keratin-specific proteases (i.e., keratinases) and the hydrolysis of keratin-rich residual biomass both take place during the same stage of the bioprocess and, as a consequence, occur simultaneously under suboptimal conditions. In the present study the keratinolytic actinomycete Amycolatopsis keratiniphila D2 was successfully employed to biodegrade thermally pretreated porcine bristles at high solids loading (16% w/v) via a novel cultivation methodology. Indeed, the two-stage submerged fermentation process developed in this work enabled to efficiently recover, in a single unit operation, about 73% of the protein material contained in the keratinous biowaste structure, resulting in an overall accumulation of 89.3 g·L−1 protein-rich hydrolysate and a productivity of 427 mg crude soluble proteins per litre per hour. The obtained protein hydrolysate powder displayed a 2.2-fold increase in its in vitro pepsin digestibility (95%) with respect to the non-hydrolysed pretreated substrate (43%). In addition, the chromatogram obtained by size-exclusion chromatography analysis of the final product indicated that, among the identified fractions, those consisting of small peptides and free amino acids were the most abundantly present inside the analysed sample. Given these facts it is possible to conclude that the soluble proteins, peptides and free amino acids recovered through the newly designed two-stage bioextraction process could represent a viable alternative source of protein in animal feed formulation.

KW - Pretreated pig bristle

KW - Amycolatopsis keratiniphila

KW - Two-stage bioprocess

KW - Keratin biodegradation

KW - Keratinolytic protease

KW - Bristle protein hydrolysate

U2 - 10.1016/j.wasman.2019.03.067

DO - 10.1016/j.wasman.2019.03.067

M3 - Journal article

C2 - 31079763

VL - 89

SP - 94

EP - 102

JO - Waste Management

JF - Waste Management

SN - 0956-053X

ER -