Arylsulphatase activity in milk and rennet from different sources

Kilic, Meral; Lindsay, R.C.

doi:10.1016/j.idairyj.2005.01.005

Cited by 6 publications

(1 citation statement)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, Kilic and Lindsay (2006) showed that pasteurization reduced arylsulphatase activity that could reduce hydrolysis of alkylphenols, which contribute to the enzymatic reactions that aid in producing the flavor in cheese.…”

Section: Introductionmentioning

confidence: 99%

Effect of Milk Pasteurization on Flavor Properties of Seven Commercially Available French Cheese Types

Chambers

Esteve²,

Retiveau

2010

Journal of Sensory Studies

View full text Add to dashboard Cite

Previous research on matched pairs of experimental cheese showed that heat treatment of milk affected flavor properties. However, whether pasteurization has a generalized effect or whether the effect is specific to certain cheese varieties is not known. Experienced, highly trained sensory panelists developed flavor profiles for seven commercially available French cheeses (Brie, Coulommier, Camembert, Saint Nectaire, Muenster, Chèvre and Bleu) for which versions made from pasteurized or unpasteurized milk were commercially available. Raw‐milk cheese had stronger odor properties. Soft cheeses with white rind (Brie, Coulommier, Camembert and Saint Nectaire) as well as Chèvre and Bleu were affected similarly by heat treatment of milk, but the sensory characteristics of Muenster cheese did not follow the pattern of other cheeses. These results suggest that many, but not all, cheese types show similar changes in sensory attributes as a result of using pasteurized rather than raw milk. PRACTICAL APPLICATIONS This study gives manufacturers and researchers information on flavor differences that exist between similar cheese types made from raw or pasteurized milk. Researchers and manufacturers can use that information in order to develop pasteurized‐milk cheese that has the traditional full‐flavored characteristics of its raw‐milk counterpart.

show abstract

Section: Introductionmentioning

confidence: 99%

Effect of Milk Pasteurization on Flavor Properties of Seven Commercially Available French Cheese Types

Chambers

Esteve²,

Retiveau

2010

Journal of Sensory Studies

View full text Add to dashboard Cite

show abstract

Homologous expression and biochemical characterization of the arylsulfatase from Kluyveromyces lactis and its relevance in milk processing

Stressler

Leisibach

Lutz-Wahl

et al. 2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

The industrial manufacturing process of lactose-free milk products depends on the application of commercial β-galactosidase (lactase) preparations. These preparations are often obtained from Kluyveromyces lactis. There is a gene present in the genome of K. lactis which should encode for an enzyme called arylsulfatase (EC 3.1.6.1). Therefore, this enzyme could also be present in β-galactosidase preparations. The arylsulfatase is suspected of being responsible for an unpleasant "cowshed-like" off-flavor resulting from the release of p-cresol from milk endogenous alkylphenol sulfuric esters. So far, no gene/functionality relationship is described. In addition, no study is available which has shown that arylsulfatase from K. lactis is truly responsible for the flavor generation. In this study, we cloned the putative arylsulfatase gene from K. lactis GG799 into the commercially available vector pKLAC2. The cloning strategy chosen resulted in a homologous, secretory expression of the arylsulfatase. We showed that the heretofore putative arylsulfatase has the desired activity with the synthetic substrate p-nitrophenyl sulfate and with the natural substrate p-cresol sulfate. The enzyme was biochemically characterized and showed an optimum temperature of 45-50 °C and an optimum pH of 9-10. Additionally, the arylsulfatase was activated by Ca(2+) ions and was inactivated by Zn(2+) ions. Moreover, the arylsulfatase was inhibited by p-cresol and sulfate ions. Finally, the enzyme was added to ultra-heat treated (UHT) milk and a sensory triangle test verified that the arylsulfatase from K. lactis can cause an unpleasant "cowshed-like" off-flavor.

show abstract

Detection, production, and application of microbial arylsulfatases

Stressler

Seitl

Kühn

et al. 2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Arylsulfatases are enzymes which catalyze the hydrolysis of arylsulfate ester bonds to release a free sulfonate. They are widespread in nature and are found in microorganisms, most animal and human tissues, and plant seeds. However, this review focuses on arylsulfatases from microbial origin and gives an overview of different assays and substrates used to determine the arylsulfatase activity. Furthermore, the production of microbial arylsulfatases using wild-type organisms as well as the recombinant production using Escherichia coli and Kluyveromyces lactis as expression hosts is discussed. Finally, various potential applications of these enzymes are reviewed.

show abstract

Arylsulphatase activity in milk and rennet from different sources

Cited by 6 publications

References 22 publications

Effect of Milk Pasteurization on Flavor Properties of Seven Commercially Available French Cheese Types

Effect of Milk Pasteurization on Flavor Properties of Seven Commercially Available French Cheese Types

Homologous expression and biochemical characterization of the arylsulfatase from Kluyveromyces lactis and its relevance in milk processing

Detection, production, and application of microbial arylsulfatases

Contact Info

Product

Resources

About