Reaction Kinetics, Mechanisms and Catalysis

, Volume 127, Issue 2, pp 583–599 | Cite as

Kluyveromyces lactis β-galactosidase immobilized on collagen: catalytic stability on batch and packed-bed reactor hydrolysis

  • Adriano Gennari
  • Francielle Herrmann Mobayed
  • André Luis Catto
  • Edilson Valmir Benvenutti
  • Giandra Volpato
  • Claucia Fernanda Volken de SouzaEmail author


The aim of this study was to evaluate the catalytic characteristics and operational stability of the tetrameric Kluyveromyces lactis β-galactosidase (KLG) enzyme immobilized on collagen. The support was submitted to four different treatments: aluminum, glutaraldehyde, acetic acid, and a combination of the methods with aluminum and glutaraldehyde. The four modified supports and the enzyme, both in its soluble and immobilized forms, were studied using thermogravimetric, differential exploratory calorimetry, infrared spectroscopy, and textural analyses. Operational pH, temperature and kinetic parameters of the soluble enzyme and of derivatives were characterized. Immobilized enzyme was applied in milk and whey lactose hydrolysis, via batch and continuous processing. There was no significant reduction (p < 0.05) in immobilization yields of all derivatives with loads up to 100 mgprotein/gsupport, with yields of approximately 70%. All derivatives reached a percentage of approximately 50% of lactose hydrolysis after 17 reuse cycles in the hydrolysis of milk and whey, using batch processing. On the other hand, hydrolysis percentages higher than 50% were achieved with packed-bed reactor even after 48 h of operation. Immobilized KLG on collagen maintained its catalytic characteristics and showed good operational stability in hydrolysis processes, especially in the continuous processes with packed-bed reactor.


Aluminum Chelator Acetic acid Glutaraldehyde Yeast 



We would like to thank Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) and Fundação de Amparo à Pesquisa do Estado do Rio Grande do Sul (FAPERGS) for the scholarships, and Universidade do Vale do Taquari - Univates for the financial support granted for this research paper. This study was financed in part by the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - Brasil (CAPES) - Finance Code 001.

Compliance with ethical standards

Conflict of interest

The authors declare they do not have any conflict of interest.


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Copyright information

© Akadémiai Kiadó, Budapest, Hungary 2019

Authors and Affiliations

  1. 1.Laboratório de Biotecnologia de Alimentos, Programa de Pós-Graduação em BiotecnologiaUniversidade do Vale do Taquari - UnivatesLajeadoBrazil
  2. 2.Centro de Ciências Exatas e TecnológicasUniversidade do Vale do Taquari - UnivatesLajeadoBrazil
  3. 3.Instituto de QuímicaUniversidade Federal do Rio Grande do SulPorto AlegreBrazil
  4. 4.Curso de Biotecnologia, Instituto Federal de EducaçãoCiência e Tecnologia do Rio Grande do Sul - IFRSPorto AlegreBrazil

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