“… -elimination of HA is usually identified only with bacterial hyaluronidases. However, the same type of hydrolysis was recently shown for the yeast Cryptococcus laurentii 7 and for the tinder fungus Fistulina hepatica 8 (Table 1 ). Figure 1 The structure of HA and the products of the hydrolysis reaction by different classes of hyaluronidases.…”
Section: Introductionsupporting
confidence: 77%
“…In this paper, we describe for the first time the hyaluronidase activity of a representative of the large group of crustaceans (Decapod order, Anomura Infraorder). At the moment, in the classification of hyaluronidases, it is considered that “certain crustacean” hyaluronidases cleave HA by -(1 3)–glycosidic bonds 7 , 8 , 16 , 44 . This statement is based on the only experimental work where the antarctic krill Euphausia superba (Euphausiacea order) hyaluronidase was studied 18 .…”
Section: Discussionmentioning
confidence: 99%
“…A50 30 44 and 6.5 HA, chondroitin sulfate A, C, D The reaction of -elimination at the -1,4-glycosidic bond, the final product is a dimer Cryptococcus laurentii 7 (yeast) 37 and 6.0 HA, ? The reaction of -elimination at the -1,4-glycosidic bond, the final product is a dimer Fistulina hepatica 8 (filamentous fungi) 20 and 4.0 HA, ? The reaction of -elimination at the -1,4-glycosidic bond, the final product is tetrasaccharide …”
Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the $$\beta $$
β
-elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases.
“… -elimination of HA is usually identified only with bacterial hyaluronidases. However, the same type of hydrolysis was recently shown for the yeast Cryptococcus laurentii 7 and for the tinder fungus Fistulina hepatica 8 (Table 1 ). Figure 1 The structure of HA and the products of the hydrolysis reaction by different classes of hyaluronidases.…”
Section: Introductionsupporting
confidence: 77%
“…In this paper, we describe for the first time the hyaluronidase activity of a representative of the large group of crustaceans (Decapod order, Anomura Infraorder). At the moment, in the classification of hyaluronidases, it is considered that “certain crustacean” hyaluronidases cleave HA by -(1 3)–glycosidic bonds 7 , 8 , 16 , 44 . This statement is based on the only experimental work where the antarctic krill Euphausia superba (Euphausiacea order) hyaluronidase was studied 18 .…”
Section: Discussionmentioning
confidence: 99%
“…A50 30 44 and 6.5 HA, chondroitin sulfate A, C, D The reaction of -elimination at the -1,4-glycosidic bond, the final product is a dimer Cryptococcus laurentii 7 (yeast) 37 and 6.0 HA, ? The reaction of -elimination at the -1,4-glycosidic bond, the final product is a dimer Fistulina hepatica 8 (filamentous fungi) 20 and 4.0 HA, ? The reaction of -elimination at the -1,4-glycosidic bond, the final product is tetrasaccharide …”
Crustacean hyaluronidases are poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we show that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed that the molecular weight of a protein with hyalorunidase activity is 40–50 kDa. Analysis of the hepatopancreas transcriptome and results of cloning and sequencing of cDNA revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. Further analysis showed that hyaluronat enzymatic cleavage follows the $$\beta $$
β
-elimination mechanism, which is well known for bacterial hyaluronidases. The results of ion-exchange chromatography showed that the final product of hyaluronate degradation is unsaturated tetrasaccharide. Thus, we identified a new hyaluronidase of higher eukaryotes, which is not integrated into the modern classification of hyaluronidases.
“…β-elimination of hyaluronate is usually identified only with bacterial hyaluronidases. However, the same type of hydrolysis was recently shown for the yeast Cryptococcus laurentii [4] and for the tinder fungus Fistulina hepatica [5] (Table 1).…”
Section: Introductionsupporting
confidence: 77%
“…Fistulina hepatica [5] (filamentous fungi) 20 and 4.0 HA, ? the reaction of β-elimination at the β-1,4-glycosidic bond, the final product is tetrasaccharide Rooster crest hyaluronate (Sigma H5338) was used to detect the hyaluronidase activity.…”
Crustacean hyaluronidases are 1 poorly understood both in terms of their enzymatic properties and in terms of their structural features. In this work, we have shown that the hepatopancreas homogenate of the red king crab has a hyaluronidase activity that is an order of magnitude higher than its commercial counterpart. Zymography revealed the hyaluronidase activity of the protein roughly from40 to 50 kDa relative to the molecular marker used in electrophoresis. Analysis of the hepatopancreas transcriptome revealed a hyaluronidase sequence with an expected molecular weight of 42.5 kDa. It turned out that the reaction of cleavage of hyaluronate in the presence of a homogenate proceeds by the mechanism of b-elimination, which is well known for bacterial hyaluronidases. Thus, a new hyaluronidase of higher eukaryotes was found and described, which is not integrated into the modern classification of hyaluronidases.
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