SU502022A1 - Acid phosphatase release method - Google Patents

Acid phosphatase release method

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Publication number
SU502022A1
SU502022A1 SU1898785A SU1898785A SU502022A1 SU 502022 A1 SU502022 A1 SU 502022A1 SU 1898785 A SU1898785 A SU 1898785A SU 1898785 A SU1898785 A SU 1898785A SU 502022 A1 SU502022 A1 SU 502022A1
Authority
SU
USSR - Soviet Union
Prior art keywords
aspergiilus
acid phosphatase
release method
protein
extraction
Prior art date
Application number
SU1898785A
Other languages
Russian (ru)
Inventor
Вия Германовна Кирсе
Анита Альфредовна Пинне
Сильвия Яновна Скуиня
Ария Мартыновна Ирген
Рута Яновна Радзиня
Original Assignee
Латвийский Филиал Всесоюзного Ордена Трудового Красного Знамени Научно-Исследовательский Институт Химических Реактивов И Особо Чистых Химических Веществ "Иреа"
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Латвийский Филиал Всесоюзного Ордена Трудового Красного Знамени Научно-Исследовательский Институт Химических Реактивов И Особо Чистых Химических Веществ "Иреа" filed Critical Латвийский Филиал Всесоюзного Ордена Трудового Красного Знамени Научно-Исследовательский Институт Химических Реактивов И Особо Чистых Химических Веществ "Иреа"
Priority to SU1898785A priority Critical patent/SU502022A1/en
Priority to FR7409536A priority patent/FR2223384A1/en
Priority to CS218674A priority patent/CS176503B1/cs
Application granted granted Critical
Publication of SU502022A1 publication Critical patent/SU502022A1/en

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    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Medicines Containing Plant Substances (AREA)
  • Medicines Containing Material From Animals Or Micro-Organisms (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)

Description

(54) СПОСОБ ВЫДЕЛЕНИЯ КИСЛОЙ ФОСФАТАЗЫ(54) METHOD FOR ISOLATING ACID PHOSPHATASE

ют. SivCTipaKHHio провод т при 5° с в течааие 1 часв. 0,1 М фосфатном буфере (,рН 7,8). -Твердую фазу отдел ют, -и белок осаждают насыщенным раствором до 80% сернокислым аммонием. Диализи1руют и лиоф.илизируют.yut. SivCTipaKHHio is conducted at 5 ° C for 1 hour. 0.1 M phosphate buffer (pH 7.8). The solid phase is separated, and the protein is precipitated with a saturated solution of up to 80% ammonium sulfate. Dialyzed and lyophilized.

Выход - 0,20 г, активность - 3,6 ед/мг npenaipaTB, 6,5 ед/мг бел«а.The output is 0.20 g, the activity is 3.6 u / mg npenaipaTB, 6.5 u / mg Bel a.

П р и м е р 4. 0,5 кг 8-дневного мнцелк  отдел ют от культуральной жидкости к размельчают . Экстрагируют гари 5° С 1 час в фосфатном буфере (1 М), рН 7,5 и осаждают белок этиловым опи1ртом - 50% -к 80%. Ос а док л и оф и л и 3 и р у ю т.PRI me R 4. 0.5 kg of an 8-day multi-compartment is separated from the culture fluid and crushed. Extraction of ashes at 5 ° C for 1 hour in phosphate buffer (1 M), pH 7.5, and precipitate the protein with ethyl alcohol - 50% to 80%. Os doc l and of l and 3 and p y t.

:Выхоа - 0,2 г, активность -1,9 ед1мг препарата, 3,0 ед/мг белка.: Vyhoa - 0.2 g, activity -1.9 u1 mg of the drug, 3.0 u / mg protein.

Пример 5. 0,6 кг 4-днев ного -мицели  отдел ют от питательной среды, промывают дза раза водой, а затем деми1нерализоза 1ной водой и гомогенизируют. Экстракци  происходит при 5° С в течение 1 час в воде, подК1ислен ной до рН 2,5, и осаждение беЛ1ка ведут пр-и насыщении сернакислым аммоние1м до 50% и 80%. Диализируют и лиофилизируют .Example 5. 0.6 kg of 4-day-wise micelles are separated from the nutrient medium, washed three times with water, and then demineralisosis with 1 water and homogenized. Extraction occurs at 5 ° C for 1 hour in water, adjusted to pH 2.5, and the precipitation of protein is carried out and saturated with ammonium sulfate 1 to 50% and 80%. Dialyzed and lyophilized.

Выход - 0,25 г, а.ктдв1Н.асть-1,5 ед/мг препарата, 2,5 ед/мг белка.The yield is 0.25 g, a.ktdv1.ast-1.5 units / mg drug, 2.5 units / mg protein.

Пр.И|Мер 6. 0,5 кг Ю-днев ного мицели  отдел ют от питательной среды « гомогенизируют . Экстракцию провод т в деминерализованной зоде при рН 6,0 и 5° С в течение 1 час. После экстракции довод т рН экстракта до 5,0 11Н NaOH. Белок осаждают до 80% насыщени  сухим сернокислым аммонием .Pr.I | Mer 6. 0.5 kg of the 10-day-old mycelium is separated from the nutrient medium and is homogenized. The extraction was carried out in demineralized zod at pH 6.0 and 5 ° C for 1 hour. After extraction, the pH of the extract was adjusted to 5.0 with 11N NaOH. The protein is precipitated to 80% saturation with dry ammonium sulphate.

Диализируют и лиофил.изируют. Выход -0,15 г, а,кти В1Ность - 2,4 ед/мгDialyzed and lyophilized. Output -0.15 g, a, KTI B1Nost - 2.4 U / mg

.препарата, 4,0 ед/мг белка..drug, 4.0 u / mg protein.

Ф О р .М у Л а и 3 о i6 р е т е 1Н и  Ф О р .М at Л a and 3 о i6 р е те 1Н and

Claims (2)

1.Способ выделени  «ислой фосфатазы из м.ицели  плесневых грибов Aspergiilus путем экстракции и осаж1дени  фер.мбнта из полученного экстракта, о т л и ч а ю щ и и с   тем, что, с целью расщирани  сырьевой базы , .выделение фоофатазы осуществл ют из плеаневых грибов, относ щихс  к виду Aspergiilus terneus.1. A method for isolating the “phosphatase layer from the Aspergiilus mold fungi micel by extracting and precipitating the ferm.bnta from the obtained extract, so that, in order to wipe out the raw material base, the extraction of photoopathase They are made from flank fungi belonging to the species Aspergiilus terneus. 2.Способ поп. 1, о т л и ч а ю щ и и с   тем, что КЗ .плесневых грибов -вида Aspergiilus terreus используют .продуценты итаконовой кислоты .2. Method pop. 1, that is, with the fact that CG of mold fungi, Aspergiilus terreus, is used by itaconic acid producers.
SU1898785A 1973-03-26 1973-03-26 Acid phosphatase release method SU502022A1 (en)

Priority Applications (3)

Application Number Priority Date Filing Date Title
SU1898785A SU502022A1 (en) 1973-03-26 1973-03-26 Acid phosphatase release method
FR7409536A FR2223384A1 (en) 1973-03-26 1974-03-20 Acid phosphatase prepn. - by aq. extraction of aspegillus terreus mycelium, fractionation with ammonium sulphate and freeze-drying
CS218674A CS176503B1 (en) 1973-03-26 1974-03-26

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
SU1898785A SU502022A1 (en) 1973-03-26 1973-03-26 Acid phosphatase release method

Publications (1)

Publication Number Publication Date
SU502022A1 true SU502022A1 (en) 1976-02-05

Family

ID=20546976

Family Applications (1)

Application Number Title Priority Date Filing Date
SU1898785A SU502022A1 (en) 1973-03-26 1973-03-26 Acid phosphatase release method

Country Status (3)

Country Link
CS (1) CS176503B1 (en)
FR (1) FR2223384A1 (en)
SU (1) SU502022A1 (en)

Also Published As

Publication number Publication date
CS176503B1 (en) 1977-06-30
FR2223384B1 (en) 1976-06-25
FR2223384A1 (en) 1974-10-25

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