Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Continuous proteolysis with a stabilized protease. II. Continuous experiments

J Boudrant, C Cheftel

    Biotechnology and Bioengineering
    |December 1, 1976
    PubMed
    Summary

    This study optimized casein-Alcalase proteolysis for soft-drink enrichment. Continuous processing with ultrafiltration allowed enzyme reuse and produced peptides under 2,000 Da, with a 0.65% threshold in orange juice.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Solubilization of phenanthrene above cloud point of Brij 30: a new application in biodegradation.

    Chemosphere·2013
    Same author

    Effect of surfactants, dispersion and temperature on solubility and biodegradation of phenanthrene in aqueous media.

    Chemosphere·2011
    Same author

    Pyrococcus abyssi alkaline phosphatase: the dimer is the active form.

    Journal of inorganic biochemistry·2004
    Same author

    Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi.

    Applied and environmental microbiology·2001
    Same author

    The effect of supplementation by different nitrogen sources on the production of lactic acid from date juice by Lactobacillus casei subsp. rhamnosus.

    Bioresource technology·2001
    Same author

    Improved performances and control of beer fermentation using encapsulated alpha-acetolactate decarboxylase and modeling.

    Biotechnology progress·2000

    Area of Science:

    • Food Science
    • Biotechnology
    • Enzyme Technology

    Background:

    • Developing protein hydrolysates for soft-drink enrichment requires specific protein-protease systems.
    • Casein and Alcalase were investigated for their suitability in creating functional hydrolysates.

    Purpose of the Study:

    • To identify an optimal protein-protease system for soft-drink hydrolysate production.
    • To characterize the kinetics and conditions for casein proteolysis by Alcalase.
    • To evaluate the feasibility of continuous proteolysis and enzyme reuse.

    Main Methods:

    • Comparative batch and continuous proteolysis experiments using casein and Alcalase.
    • Kinetic analysis, including substrate concentration effects and product inhibition.
    • Optimization of reaction conditions: pH 8.8, 5% casein concentration, 40°C.

    Related Experiment Videos

  • Ultrafiltration (PM 30 membrane) for enzyme retention and reuse.
  • Gel chromatography for peptide molecular weight determination.
  • Sensory analysis (triangular taste tests) to determine hydrolysate threshold concentration.

    • Main Results:

    • Casein-Alcalase proteolysis kinetics are influenced by substrate concentration and inhibited by reaction products.
    • Optimal reaction conditions were determined as pH 8.8, 5% casein, and 40°C.
    • The enzyme Alcalase (43,000 Da) was effectively retained using a PM 30 ultrafiltration membrane.
    • Continuous proteolysis enabled enzyme reuse for seven days at 40°C with minimal microbial growth.
    • Generated peptides had a molecular weight range below 2,000 Da.
    • The dry hydrolysate had a threshold identification concentration of approximately 0.65% in orange juice.

    Conclusions:

    • The casein-Alcalase system, under optimized conditions with ultrafiltration, is suitable for producing soft-drink enriching hydrolysates.
    • Continuous processing facilitates enzyme reusability and microbial inhibition, enhancing process efficiency.
    • The resulting hydrolysate peptides are small (<2,000 Da) and exhibit a low sensory threshold in beverages.