View in EDS

Valorization of protein-rich waste for industrial enzyme production: Purification and cheese making performance of a novel milk clotting protease from Streptomyces thermolineatus GZ1B10.

Saved in:
Bibliographic Details
Title: Valorization of protein-rich waste for industrial enzyme production: Purification and cheese making performance of a novel milk clotting protease from Streptomyces thermolineatus GZ1B10.
Authors: Dahdah, Kamal1 (AUTHOR), Zikiou, Abdellah1 (AUTHOR) a.zikiou@crbt.dz, Zaamta, Maya Fariel2 (AUTHOR), Mechati, Fedoua2 (AUTHOR), Fiala, Samah1 (AUTHOR), Saci, Fairouz1 (AUTHOR)
Source: World Journal of Microbiology & Biotechnology. Jun2026, Vol. 42 Issue 6, p1-13. 13p.
Subjects: Streptomyces, Cheesemaking, Proteolytic enzymes, Proteolysis, Organic wastes, Industrial enzymology, Coagulation (Food science), Thermal stability
Abstract: Proteases from the genus Streptomyces exhibit diverse biochemical properties with significant industrial potential. This study explores the valorization of protein rich waste as a substrate for the production, purification, and characterization of a novel milk clotting protease from the endophytic isolate GZ1B10, recovered from wild Beta vulgaris tubers. Molecular identification based on 16 S rDNA sequencing revealed 99.75% similarity to Streptomyces thermolineatus. The extracellular protease was purified by size exclusion chromatography followed by desalting, yielding 10.51 ± 0.8 mg of homogeneous enzyme. SDS-PAGE analysis revealed a single protein band with an estimated molecular weight of 21.8 kDa. Purification enhanced milk clotting activity (14.55 to 85.12 RU) and specific activity (0.21 to 8.09 RU/mg), approaching the activity profile of commercial rennet. Casein hydrolysis assays indicated selective κ-casein degradation (72%) supporting a rennet-like mode of action. Both crude and purified proteases exhibited optimal coagulation at pH 5.5, 60 °C, and 0.03 M CaCl₂, indicating high thermostability compared with rennet. Cheese yield measurements showed comparable results (16.25 g/100 mL) with similar syneresis (34.25%) and slightly improved moisture retention. This study reports S. thermolineatus as an endophyte of wild B. vulgaris for the first time and presents, to our knowledge, the first evidence of milk clotting protease production by this species, highlighting its potential as an alternative coagulant for industrial cheese production. [ABSTRACT FROM AUTHOR]
Copyright of World Journal of Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 194750147
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Valorization of protein-rich waste for industrial enzyme production: Purification and cheese making performance of a novel milk clotting protease from Streptomyces thermolineatus GZ1B10.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Dahdah%2C+Kamal%22">Dahdah, Kamal</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zikiou%2C+Abdellah%22">Zikiou, Abdellah</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> a.zikiou@crbt.dz</i><br /><searchLink fieldCode="AR" term="%22Zaamta%2C+Maya+Fariel%22">Zaamta, Maya Fariel</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Mechati%2C+Fedoua%22">Mechati, Fedoua</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Fiala%2C+Samah%22">Fiala, Samah</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Saci%2C+Fairouz%22">Saci, Fairouz</searchLink><relatesTo>1</relatesTo> (AUTHOR)
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22World+Journal+of+Microbiology+%26+Biotechnology%22">World Journal of Microbiology & Biotechnology</searchLink>. Jun2026, Vol. 42 Issue 6, p1-13. 13p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Streptomyces%22">Streptomyces</searchLink><br /><searchLink fieldCode="DE" term="%22Cheesemaking%22">Cheesemaking</searchLink><br /><searchLink fieldCode="DE" term="%22Proteolytic+enzymes%22">Proteolytic enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Proteolysis%22">Proteolysis</searchLink><br /><searchLink fieldCode="DE" term="%22Organic+wastes%22">Organic wastes</searchLink><br /><searchLink fieldCode="DE" term="%22Industrial+enzymology%22">Industrial enzymology</searchLink><br /><searchLink fieldCode="DE" term="%22Coagulation+%28Food+science%29%22">Coagulation (Food science)</searchLink><br /><searchLink fieldCode="DE" term="%22Thermal+stability%22">Thermal stability</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Proteases from the genus Streptomyces exhibit diverse biochemical properties with significant industrial potential. This study explores the valorization of protein rich waste as a substrate for the production, purification, and characterization of a novel milk clotting protease from the endophytic isolate GZ1B10, recovered from wild Beta vulgaris tubers. Molecular identification based on 16 S rDNA sequencing revealed 99.75% similarity to Streptomyces thermolineatus. The extracellular protease was purified by size exclusion chromatography followed by desalting, yielding 10.51 ± 0.8 mg of homogeneous enzyme. SDS-PAGE analysis revealed a single protein band with an estimated molecular weight of 21.8 kDa. Purification enhanced milk clotting activity (14.55 to 85.12 RU) and specific activity (0.21 to 8.09 RU/mg), approaching the activity profile of commercial rennet. Casein hydrolysis assays indicated selective κ-casein degradation (72%) supporting a rennet-like mode of action. Both crude and purified proteases exhibited optimal coagulation at pH 5.5, 60 °C, and 0.03 M CaCl₂, indicating high thermostability compared with rennet. Cheese yield measurements showed comparable results (16.25 g/100 mL) with similar syneresis (34.25%) and slightly improved moisture retention. This study reports S. thermolineatus as an endophyte of wild B. vulgaris for the first time and presents, to our knowledge, the first evidence of milk clotting protease production by this species, highlighting its potential as an alternative coagulant for industrial cheese production. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of World Journal of Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=194750147
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1007/s11274-026-05043-4
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 13
        StartPage: 1
    Subjects:
      – SubjectFull: Streptomyces
        Type: general
      – SubjectFull: Cheesemaking
        Type: general
      – SubjectFull: Proteolytic enzymes
        Type: general
      – SubjectFull: Proteolysis
        Type: general
      – SubjectFull: Organic wastes
        Type: general
      – SubjectFull: Industrial enzymology
        Type: general
      – SubjectFull: Coagulation (Food science)
        Type: general
      – SubjectFull: Thermal stability
        Type: general
    Titles:
      – TitleFull: Valorization of protein-rich waste for industrial enzyme production: Purification and cheese making performance of a novel milk clotting protease from Streptomyces thermolineatus GZ1B10.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Dahdah, Kamal
      – PersonEntity:
          Name:
            NameFull: Zikiou, Abdellah
      – PersonEntity:
          Name:
            NameFull: Zaamta, Maya Fariel
      – PersonEntity:
          Name:
            NameFull: Mechati, Fedoua
      – PersonEntity:
          Name:
            NameFull: Fiala, Samah
      – PersonEntity:
          Name:
            NameFull: Saci, Fairouz
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 06
              Text: Jun2026
              Type: published
              Y: 2026
          Identifiers:
            – Type: issn-print
              Value: 09593993
          Numbering:
            – Type: volume
              Value: 42
            – Type: issue
              Value: 6
          Titles:
            – TitleFull: World Journal of Microbiology & Biotechnology
              Type: main
ResultId 1