O uso das enzimas na indústria de laticínios: uma breve revisão

Marciel Dela Justina, Mariléia Buss Dela Justina, Everton Skoronski

Resumo


O principal objetivo do presente trabalho é fornecer uma visão geral sobre os aspectos técnicos da utilização de enzimas no processamento do leite. Enzimas indicadoras de processo, como a fosfatase alcalina e a lactoperoxidase, são utilizadas na validação do tratamento térmico do leite. Contudo, o desenvolvimento de novas técnicas para controle microbiológico do leite representa um desafio para a manutenção da sua usabilidade. Novas fontes de enzimas coagulantes têm sido estudadas. A imobilização enzimática tem sido estudada com o intuito de aumentar a sua estabilidade, período de estocagem, e número de usos na produção de laticínios. O estudo da imobilização enzimática é realizado visando várias finalidades na indústria de laticínios, entre elas a coagulação e a hidrólise. O uso de enzimas encapsuladas é importante para a maturação de queijos, prevenindo a deterioração de textura ou de sabor durante este período.

Palavras-chave


enzimas do leite; lipólise; proteólise; coagulação do leite; maturação do queijo.

Texto completo:

PDF

Referências


AHMED, S. A. et al. Novel milk-clotting enzyme from Bacillus stearothermophilus as a coagulant in UF-white soft cheese. Biocatalysis and Agricultural Biotechnology, v. 7, p. 241-249, 2016.

AY, M.; BOSTAN, K. Effects of Activated Lactoperoxidase System on Microbiological Quality of Raw Milk. Kafkas universitesi veteriner fakultesidergisi, v. 23, n. 1, p. 131-136, 2017.

BAROUNI, E. et al. Tubular cellulose/starch gel composite as food enzyme storehouse. Food Chemistry, v. 188, p. 106-110, 2015.

BOOTS, J. W.; FLORIS, R. Lactoperoxidase: From catalytic mechanism to practical applications. International Dairy Journal, v. 16, n. 11, p. 1272-1276, 2006.

BOULARES, M.; MANKAI, M.; HASSOUNA, M. Effect of activating lactoperoxidase system in cheese milk on the quality of Saint-Paulin cheese. International Journal of Dairy Technology, v. 64, n. 1, p. 75-83, 2011.

CAMPBELL, R. E.; DRAKE, M. A. Invited review: The effect of native and nonnative enzymes on the flavor of dried dairy ingredients. Journal of Dairy Science, v. 96, n. 8, p. 4773-4783, 2013.

CENI, G. et al. Continuous inactivation of alkaline phosphatase and Escherichia coli in milk using compressed carbon dioxide as inactivating agent. Biochemical Pharmacology, v. 13, p. 24-28, 2016.

CHEN, Y. C.; CHEN, C. C.; HSIEH, J. F. Propylene glycol alginate-induced coacervation of milk proteins: A proteomics approach. Food Hydrocolloids, v. 53, p. 233-238, 2016.

DALGLEISH, D. G.; CORREDIG, M. The Structure of the Casein Micelle of Milk and Its Changes During Processing. Annual Review of Food Science and Technology, v. 3, n. 1, p. 449-467, 2012.

DARIO, A. et al. The quality of low lactose milk is affected by the side proteolytic activity of the lactase used in the production process. Food Research International, v. 89, p. 514525, 2016.

DUMITRAŞCU, L. et al. Thermal inactivation of lactoperoxidase in goat, sheep and bovine milk – A comparative kinetic and thermodynamic study. Journal of Food Engineering, v. 113, n. 1, p. 47-52, 2012.

EGGER, L.; NICOLAS, M.; PELLEGRINO, L. Alkaline phosphatase activity in cheese as a tracer for cheese milk pasteurization. LWT – Food Science and Technology, v. 65, p. 963-968, 2016.

ESPOSITO, M. et al. Enzymatic milk clotting activity in artichoke (Cynara scolymus) leaves and alpine thistle (Carduus defloratus) flowers. Immobilization of alpine thistle aspartic protease. Food Chemistry, v. 204, p. 115-121, 2016.

FARRELL, H. M. et al. Casein micelle structure: What can be learned from milk synthesis and structural biology? Current Opinion in Colloid & Interface Science, v. 11, n. 2-3, p. 135-147, 2006.

FERNANDES, P. Enzymes in food processing: A condensed overview on strategies for better biocatalysts. Enzyme Research, v. 2010, n. 1, 862537, 2010.

GARG, G.; SEHRAWAT, N.; YADAV, M. Role of Enzymes in Food Industries. Frontiers in Food Biotechnology. In: SHARMA, C., SHARMA A. K., ANEJA, K. R. Frontiers in Food Biotechnology, 1ª ed. New York: Nova Publishers, 2016. cap. 9, p. 219-252.

GAUCHER, I. et al. Physico-chemical characterization of phosphate-added skim milk. International Dairy Journal, v. 17, n. 12, p. 1375-1383, 2007.

GÜLER­AKIN, M. B. et al. Accelerated kashar cheese ripening with encapsulated lipase and protease enzymes. Italian Journal of Food Science, v. 24, n. 4, p. 358-366, 2012.

HRISTOV, P. et al. Measurement of Casein Micelle Size in Raw Dairy Cattle Milk by Dynamic Light Scattering. In: Milk Proteins – From Structure to Biological Properties and Health Aspects. Published: September 7th, 2016. DOI:10.5772/60465. ISBN: 978953-51-2537-2.

INNOCENTE, N. et al. Effect of pulsed light on total microbial count and alkaline phospha tase activity of raw milk. International Dairy Journal, v. 39, n. 1, p. 108-112, 2014.

JACOB, M.; JAROS, D.; ROHM, H. Recent advances in milk clotting enzymes. International Journal of Dairy Technology, v. 64, n. 1, p. 14-33, 2011.

JANSSON, T. et al. Lactose-Hydrolyzed milk is more prone to chemical changes during storage than conventional Ultra High-Temperature (UHT) Milk. Journal of Agricultural and Food Chemistry, v. 62, p. 7886-7896, 2014.

KIM, D. et al. Establishing quantitative standards for residual alkaline phosphatase in pasteurized milk. Korean Journal for Food Science of Animal Resources, v. 36, n. 2, p. 194-197, 2016.

KLEIN, M. P.; JONG, E. V. DE; RÉVILLION, J. P. P. Utilização da Beta-galactosidase para prevenção da cristalização em doce de leite. Ciência e Tecnologia de Alimentos, v. 34, n. 6, p. 1530-1535, 2010.

KUMARI, A. et al. Isolation and immobilization of alkaline protease on mesoporous silica and mesoporous ZSM-5 zeolite materials for improved catalytic properties. Biochemistry and Biophysics Reports, v. 2, p. 108-114, 2015.

KUSSENDRAGER, K. D.; HOOIJDONK, A. C. M. VAN. Lactoperoxidase: physicochemical properties , occurrence, mechanism of action and applications. British Journal of Nutrition, v. 84, n. 1, p. 19-25, 2000.

LEMES, A. C. et al. A new milk-clotting enzyme produced by Bacillus sp. P45 applied in cream cheese development. LWT – Food Science and Technology, v. 66, p. 217-224, 2016.

LORENZEN, P. C. et al. Activities of alkaline phosphatase, gamma-glutamyltransferase and lactoperoxidase in cow, sheep and goat’ s milk in relation to heat treatment. Small Ruminant Research, v. 89, p. 18-23, 2010.

MATTANNA, P. et al. Parâmetros tecnológicos e sensoriais de requeijões cremosos com baixo teor de lactose. Revista do Instituto de Laticínios Cândido Tostes, v. 387, n. 67, p. 30-37, 2012.

MCSWEENEY, P. L. H. Biochemistry of cheese ripening. International Journal of Dairy Technology, v. 57, n. 2-3, p. 127-144, 2004.

NARWAL, R. K. et al. Inactivation thermodynamics and iso-kinetic profiling for evaluating operational suitability of milk clotting enzyme immobilized in composite polymer matrix. International Journal of Biological Macromolecules, v. 91, p. 317328, 2016.

O’RIORDAN, N. et al. Structural and functional characteristics of bovine milk protein glycosylation. Glycobiology, v. 24, n. 3, p. 220-236, 2014.

PANESAR, P. S.; KUMARI, S.; PANESAR, R. Potential Applications of Immobilized β ­Galactosidase in Food Processing Industries. Enzime Research, v. 2010, 2010.

PEREIRA, M. C. S. et al. Lácteos com baixo teor de lactose: Uma necessidade para portadores de má digestão da lactose e um nicho de mercado. Revista do Instituto de Laticínios Cândido Tostes, v. 389, n. 67, p. 57-65, 2012.

PINHO, C. R. G.; FRANCHI, M. A.; TRIBST, A. A. L. Effect of ultra high pres sure homogenization on alkaline phosphatase and lactoperoxidase activity in raw skim milk. Italian Oral Surgery, v. 1, p. 874-878, 2011.

RANKIN, S. A. et al. Invited review: The application of alkaline phosphatase assays for the validation of milk product pasteurization. Journal of Dairy Science, v. 93, n. 12, p. 5538-5551, 2010.

SEIFU, E.; BUYS, E. M.; DONKIN, E. F. Quality aspects of Gouda cheese made from goat milk preserved by the lactoperoxidase system. International Dairy Journal, v. 14, p. 581-589, 2004.

SEIFU, E.; BUYS, E. M.; DONKIN, E. F. Significance of the lactoperoxidase system in the dairy industry and its potential applications: A review. Trends in Food Science and Technology, v. 16, n. 4, p. 137154, 2005.

SHAMILA­SYUHADA, A. K.; CHUAH, L.; WAN-NADIAH, W. A. Inactivation of microbiota and selected spoilage and pathogenic bacteria in milk by combinations of ultrasound, hydrogen peroxide , and active lactoperoxidase system. International Dairy Journal, v. 61, p. 120-125, 2016.

SILVA, R. R. da et al. Biochemical and milk clotting properties and mapping of catalytic subsites of an extracellular aspartic peptidase from basidiomycete fungus Phanerochaete chrysosporium. Food Chemistry, v. 225, p. 45-54, 2017.

SOSNOWSKI, M.; ROLA, J. G.; OSEK, J. Alkaline phosphatase activity and microbiological quality of heat-treated goat milk and cheeses. Small Ruminant Research, v. 136, p. 132-136, 2016.

TAYEFI-NASRABADI, H.; HOSEINPOURFAYZI, M. A.; MOHASSELI, M. Effect of heat treatment on lactoperoxidase activity in camel milk: A comparison with bovine lactoperoxidase. Small Ruminant Research, v. 99, n. 2-3, p. 187-190, 2011.

TREMONTE, P. et al. Raw milk from ven ding machines: Effects of boiling, microwave treatment, and refrigeration on microbiological quality. Journal of Dairy Science, v. 97, n. 6, p. 3314-3320, 2014.

TRUJILLO, A. J.; POZO, P. I.; GUAMIS, B. Effect of heat treatment on lactoperoxidase activity in caprine milk. Small Ruminant Research, v. 67, p. 243-246, 2007.

UPADHYAY, L. S. B.; VERMA, N. A three step approach for the purification of alkaline phosphatase from non-pasteurized milk. Journal of Food Science and Technology, v. 52, n. May, p. 3140-3146, 2014.

WILIŃSKA, A. et al. Kinetics of thermal inactivation of alkaline phosphatase in bovine and caprine milk and buffer. International Dairy Journal, v. 17, n. 6, p. 579-586, 2007.

YEGIN, S.; DEKKER, P. Progress in the field of aspartic proteinases in cheese manufacturing: Structures, functions, catalytic mechanism, inhibition, and engineering. Dairy Science and Technology, v. 93, n. 6, p. 565594, 2013.

YONG, L. et al. Investigation of concentration of thiocyanate ion in raw cow’s milk from China, New Zealand and the Netherlands. Food Chemistry, v. 215, p. 61-66, 2017.

YU, L. et al. Biosensors and Bioelectronics Disposable lateral flow­through strip for smartphone-camera to quantitatively detect alkaline phosphatase activity in milk. Biosensors and Bioelectronic, v. 69, p. 307315, 2015.




DOI: https://doi.org/10.14295/2238-6416.v73i3.679

Apontamentos

  • Não há apontamentos.


Licença Creative Commons
Esta obra está licenciada com uma Licença Creative Commons Atribuição 4.0 Internacional.