Comparative electrophoresis and some properties of alkaline proteinases produced by Monascus spp.

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.

show abstract

Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

Yasuda

Tachibana

Kuba-Miyara

2012

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

A trypsin-like serine proteinase from plasmodial membrane of Physarum polycephalum.

Morita

Kan

Sugano

et al. 1996

J. Gen. Appl. Microbiol.

View full text Add to dashboard Cite

A trypsin-like serine proteinase was found in a plasma membrane fraction from the plasmodia of Physarum polycephalum. It was solubilized from the plasma membrane fraction with 1% (w/v) Triton X-100 and purified by a series of column chromatographic steps followed by polyacrylamide gel electrophoresis (PAGE). The molecular mass of the enzyme was estimated to be 130 kDa by SDS-PAGE under non-reducing conditions. This enzyme exhibited maximal activity at pH 9 and at 35°C with the substrate Boc-Phe-Ser-Arg-MCA, and was sensitive to various serine proteinase inhibitors and trypsin inhibitors. The enzyme was significantly labeled with [3H]diisopropylfluorophosphate (DFP); however, a clear decrease in the amount of the enzyme bound-[3H]DFP was observed in the presence of p-nitrophenyl p'-guanidinobenzoate (NPGB), an active site titrant for trypsin. The activity was completely inhibited in the presence of EDTA or EGTA, but the metal-depleted enzyme was reactivated by the addition of Cart Moreover, this enzyme was capable of cleaving several synthetic peptides at the carboxyl side of arginine, but did not work on synthetic substrates for chymotrypsin, elastase and aminopeptidase. The enzyme showed an affinity to Con A, indicating that it contains a carbohydrate moiety. Inhibition of the activity by a serine proteinase inhibitor resulted in cessation of the DNA synthesis in growing plasmodia without loss of the protein synthesis. Thus, this trypsin-like serine proteinase may have a regulatory role in the growth and development of the slime mould.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Comparative electrophoresis and some properties of alkaline proteinases produced by Monascus spp.

Cited by 2 publications

References 12 publications

Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

A trypsin-like serine proteinase from plasmodial membrane of Physarum polycephalum.

Contact Info

Product

Resources

About