Religiosin B, a milk-clotting serine protease from Ficus religiosa

被引：38

作者：

Kumari, Moni ^{[1
]}

Sharma, Anurag ^{[1
]}

Jagannadham, M. V. ^{[1
]}

机构：

[1] Banaras Hindu Univ, Inst Med Sci, Mol Biol Unit, Varanasi 221005, Uttar Pradesh, India

来源：

FOOD CHEMISTRY | 2012年 / 131卷 / 04期

关键词：

Ficus religiosa; Latex; Milk-clotting enzyme; Religiosin B; Serine protease; CYNARA-CARDUNCULUS; BIOCHEMICAL-CHARACTERIZATION; CYSTEINE PROTEASE; PURIFICATION; ENZYME; LATEX; CUCUMISIN; SARCOCARP; SEEDS;

D O I：

10.1016/j.foodchem.2011.09.122

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

A novel milk-clotting serine protease, named religiosin B, is purified from Ficus religiosa. The molecular mass of the protein is 63,000 with pI value of pH 7.6. The proteolytic activity of the enzyme is strongly inhibited by phenylmethanesulfonyl fluoride (PMSF) and chymostatin. Religiosin B acts optimally at pH 8.0-8.5 and temperature 55 degrees C. The molar absorption coefficient of the enzyme is 149,725 M-1 cm(-1) with 23 tryptophan, 15 tyrosine and 7cysteine residues per molecule of the enzyme. The enzyme shows broad substrate specificity with natural as well as synthetic substrates. Religiosin B is highly stable against denaturants and metal ions as well as over a wide range of pH and temperature. The de novo sequencing confirms the novelty of the enzyme. In addition to its high milk-clotting ability, it could be used in the cheese industry, as well as other food and biotechnological industries. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：1295 / 1303

页数：9

共 33 条

[1] PRODUCTION AND SOME PROPERTIES OF RENNIN-LIKE MILK-CLOTTING ENZYME FROM PENICILLIUM-CITRINUM [J].

ABDELFATTAH, AF ;

MABROUK, SS ;

ELHAWWAR.NM .

JOURNAL OF GENERAL MICROBIOLOGY, 1972, 70 (APR) :151-+

[2] pH stability and influence of salts on activity of a milk-clotting enzyme from Solanum dubium seeds and its enzymatic action on bovine caseins [J].

Ahmed, Isam A. Mohamed ;

Babiker, Elfadil E. ;

Mori, Nobuhiro .

LWT-FOOD SCIENCE AND TECHNOLOGY, 2010, 43 (05) :759-764

[3] Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen [J].

Ahmed, Isam A. Mohamed ;

Morishima, Isao ;

Babiker, Elfadil E. ;

Mori, Nobuhiro .

PHYTOCHEMISTRY, 2009, 70 (04) :483-491

[4] Characterisation of partially purified milk-clotting enzyme from Solanum dubium Fresen seeds [J].

Ahmed, Isam Ali Mohamed ;

Morishima, Isao ;

Babiker, Elfadil E. ;

Mori, Nobuhiro .

FOOD CHEMISTRY, 2009, 116 (02) :395-400

[5] Effect of pH at heat treatment on the hydrolysis of κ-casein and the gelation of skim milk by chymosin [J].

Anema, Skelte G. ;

Lee, Slew Kim ;

Klostermeyer, Henning .

LWT-FOOD SCIENCE AND TECHNOLOGY, 2007, 40 (01) :99-106

[6] Cleavage specificity of cucumisin, a serine protease, with synthetic substrates [J].

Arima, K ;

Yonezawa, H ;

Uchikoba, T ;

Shimada, M ;

Kaneda, M .

PHYTOCHEMISTRY, 2000, 54 (05) :451-454

[7]

Arima K., 1970, Methods Enzymol, V19, P446, DOI DOI 10.1016/0076-6879(70)19033-1

[8] Purification and characterization of a serine protease from Cucumis trigonus Roxburghi [J].

Asif-Ullah, Mufti ;

Kim, Key-Sun ;

Yu, Yeon Gyu .

PHYTOCHEMISTRY, 2006, 67 (09) :870-875

[9]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[10]

Dubey VK, 2003, PHYTOCHEMISTRY, V62, P1057, DOI 10.1016/S0031-9422(02)00676-3

← 1 2 3 4 →