The extracellular proteolytic enzymes of the mosquito-parasitizing fungus Lagenidium giganteum

Dean, David D.; Domnas, A.

doi:10.1016/0147-5975(83)90072-5

Cited by 23 publications

(9 citation statements)

References 32 publications

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“…Thus, cross-checking of different enzyme preparations should be done using the same batch of Azocoll. The method using Azocoll was similar to that of Dean and Domnas (1983). Enzyme was added to buffer at the appropriate pH to obtain a total volume of 5.0 ml.…”

Section: Methodsmentioning

confidence: 99%

Liquifying Cod Fish Frames Under Acidic Conditions With a Fungal Enzyme

Ferreira

Hultin

1994

J Food Processing Preservation

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An acidic protease (Newlase A from Rhizopus niveus, Amano) was evaluated as to its ability to reduce viscosity of ground cod fish frames without excessive hydrolysis. Newlase A had an optimal pH of 3.5 and an optimal temperature of 60C with Azocoll as substrate. the enzyme was more stable in the ground fish mixture at pH 3.5 than it was in citrate:phosphate buffer of the same pH. the enzyme hydrolyzed the fish proteins more extensively and decreased the viscosity of the ground fish more between 40–50C over an extended time period than at its optimal temperature of 60C. It is likely that the lower optimal temperature under these conditions is related to its greater stability at the lower temperatures. the energy of activation of the deactivation of the enzyme was 44.5 Kcal per mol‐degree. Over a period of 75 min at 45C there was a decrease in viscosity of the ground fish with added enzyme of some two orders of magnitude. After a 3‐h incubation, total soluble protein increased from 30% to 48%; the amount of each molecular size fraction produced decreased in the following order: 1–3, < 10, < 1, and 3–10 kdaltons.

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Section: Methodsmentioning

confidence: 99%

Liquifying Cod Fish Frames Under Acidic Conditions With a Fungal Enzyme

Ferreira

Hultin

1994

J Food Processing Preservation

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“…A synthetic substrate, Azocoll (Calbiochem-Novabiochem, La Jolla, CA), was used to estimate the general proteolyhc activity of the caeca extract based upon the methods of Dean and Domnas (1 983) and Ferreira and Hultin (1994), with some modification. Exactly 50 mg of Azocoll was added to 0.1 N sodium phosphate buffer @H 7.5) to give a total volume of 5.0 mL in spectrophotometer glass tubes.…”

Section: Enzyme Activity Assaysmentioning

confidence: 99%

Hydrolysis of Salmon Muscle Proteins by an Enzyme Mixture Extracted From Atlantic Salmon (Salmo Salar) Pyloric Caeca

Kristinsson

Rasco

2000

J Food Biochemistry

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An expact of serine proteasespom the pyloric caeca of Atlantic salmon (Salmo salar) was recovered by (NHJJO, and stabilized in 20% glycerol. Proteolytic activity was determined using Azocoll and hydrolytic eficiency evaluated on salmon muscle mince. Activity assays identijied chymotrypsin as the most active serine protease component, followed by trypsin and elastase. The caeca extract more eficiently hydrolyzed a salmon muscle mince substrate at 40C compared to 21.5C, and was very eficient compared to four commercial protease preparations in terms of degrees of hydrolysis (OH) achieved ajier a 180 min reaction. Salmon protein hydrolysates made from the enzymatic hydrolysis with the pyloric caeca enzymes had digerent peptide profiles at the same DH when the reaction took place at 21.5C compared to 40C, suggesting that relative activities of these serine proteases may be different at dgferent reaction temperatures.Commercially available enzymes fiom a variety of sources have been used to make 'Present address:

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“…The production of cuticle-degrading enzymes, proteases, chitinases, and lipases, has long been recognized as an important determinant of the infection process in various fungi, facilitating penetration as well as providing nourishment for further development (Charnley, 1984;Dean and Domnas, 1983;Samsináková et al, 1971). A study by using Heliothis zea "larval ghosts" demonstrated that a sequence of proteinase followed by chitinase enzymatic digests was needed to dissolve the insect cuticle.…”

Section: Infection Processes and Pathogenicitymentioning

confidence: 98%