Purification and Properties of a Ribonuclease from a Species of the Genus<i>Monascus</i>

Red koji or red mold rice is prepared by growing a genus Monascus on steamed rice. For centuries, it has been used in Asia for the production of fermented foods including red rice wine and fermented tofu. Although red koji is an important source of various hydrolytic enzymes critical for food fermentation, information on the enzymatic properties in red koji has been limited. Hydrolytic enzymes produced by Monascus fungi may play important roles in ripening of tofuyo (Japanese fermented tofu) regarding the chemical and physical properties of the product. This review provides an introduction of red koji, its properties, and the application of hydrolytic enzymes, especially aspartic proteinases and carboxypeptidases from Monascus fungi. We also describe tofuyo and a novel fermented soybean protein food using a microbial action originating from red koji.

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Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

Yasuda

Tachibana

Kuba-Miyara

2012

Appl Microbiol Biotechnol

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Purification, kinetic and thermodynamic studies of a new ribonuclease from a mutant of Aspergillus niger

Xiong¹,

Liu²,

Song³

et al. 2005

Journal of Biotechnology

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Purification and Partial Characterization of an Extracellular Ribonuclease From a Mutant of <I>Aspergillus niger</I>

Xiong¹,

Liu²,

Song³

2005

ABAB

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A new extracellular ribonuclease (RNase) from a mutant of Aspergillus niger, named A. niger SA-13-20 RNase, was purified to homogeneity by (NH4)2SO4 fractionation (50-85%), DEAE-cellulose anion-exchange chromatography, ultrafiltration and Sephacryl HR-200 chromatography. The enzyme was purified up to 54.4-fold with a final yield of 24.5%. There were differences in the molecular weight, pI value and some physico-chemical properties between A. niger SA-13-20 RNase and that from the parent strain. The enzyme is monomeric and its molecular weight and isoelectric point were 40.1 kDa and 5.3, respectively. The N-terminal amino acid sequence of A. niger SA-13-20 RNase was TIDTYSSDSP. The optimum pH, temperature and buffer concentration for the enzymatic reaction were 3.5, 65 degrees C, and 0.175 M, respectively. Metal ions, such as K+, NH4+, Mg2+, and Ca2+ at the concentration of 1.0 mM had a slight activation effect on the enzyme activity and (NH4)2SO4 activated the enzyme significantly. The enzyme was stable at pH lower than 8.5 and was easy to inactivate in strong alkali solution.

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Purification and Properties of a Ribonuclease from a Species of the GenusMonascus

Cited by 3 publications

References 8 publications

Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

Purification, kinetic and thermodynamic studies of a new ribonuclease from a mutant of Aspergillus niger

Purification and Partial Characterization of an Extracellular Ribonuclease From a Mutant of <I>Aspergillus niger</I>

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