Expression of key hydrolases for soy sauce fermentation in Zygosaccharomyces rouxii

Yuzuki, Masanobu; Matsushima, Kiyoshi; Koyama, Yasuji

doi:10.1016/j.jbiosc.2014.06.015

Cited by 15 publications

(5 citation statements)

References 8 publications

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“…Proteases, especially the neutral protease, make up the largest proportion of industrial enzymes around the world (Kasana et al 2011 ). Neutral proteases are widely applied in the food (Tavano 2013 ; Yuzuki et al 2015 ), feed (Zhang et al 2014 ), pharmaceutical (Umeadi et al 2008 ) and leather (Asker et al 2013 ) industries because of their distinct benefits, including a mild catalysis process, low pollution level and high yield. In the food industry, the neutral protease is generally used for debittering soy sauce (Machida et al 2005 ) and brewing beer (Wang et al 2013 ).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of neutral protease from Aspergillus oryzae Y1 isolated from naturally fermented broad beans

et al. 2018

AMB Expr

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The strain Y1, with a notably high production of neutral protease, was isolated from naturally fermented broad beans and subsequently identified as Aspergillus oryzae, through the analysis of its morphology characteristics and 18S rDNA sequence. Naturally fermented broad beans are the main raw material in Sichuan broad-bean sauce. The neutral protease from Aspergillus oryzae Y1 was purified using ammonium sulphate precipitation and DEAE-Sepharose Fast Flow chromatography, which resulted in a 10.0-fold increase in the specific activity (2264.3 U/mg) and a recovery rate of 21%. The estimated molecular mass of the purified protease was approximately 45 kDa. The optimal pH and temperature of the purified protease were 7.0 and 55 °C, respectively. The heat resistance of the purified protease was significantly higher than the commercial protease. The effect of metal ions on the activity of the purified protease approximated that of commercial neutral protease. Furthermore, the maximum hydrolysis rate (Vmax) and apparent Michaelis–Menten constant (Km) values of the purified protease were 256.4103 μg/mL min and 20.0769 mg/mL, respectively. The purified protease had a higher affinity for the substrate than the commercial neutral protease. All the results suggest that this neutral protease exhibits the potential for application in industry due to its good resistance to high temperatures and wide range of acids and bases.

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Section: Introductionmentioning

confidence: 99%

Purification and characterization of neutral protease from Aspergillus oryzae Y1 isolated from naturally fermented broad beans

et al. 2018

AMB Expr

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“…The obtained mutant H8 has high STP activity and is able to significantly increase the amount of peptides and free amino acids in soy sauce. Similarly, the expression of several key hydrolase genes from Aspergillus sojae or A. oryzae , such as protease, peptidase, and glutaminase, in the salt-tolerant yeast Zygosaccharomyces rouxii not only increases the yield of STPs, but also serves as a potential means to provide additional hydrolase during soy sauce fermentation (Yuzuki et al 2015 ).…”

Section: Examples Of Microbial-derived Stps Applied To High-salt Trad...mentioning

confidence: 99%

Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review

Yao,

Liu,

Liu

et al. 2023

Bioresour. Bioprocess.

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Different microorganisms can produce different proteases, which can adapt to different industrial requirements such as pH, temperature, and pressure. Salt-tolerant proteases (STPs) from microorganisms exhibit higher salt tolerance, wider adaptability, and more efficient catalytic ability under extreme conditions compared to conventional proteases. These unique enzymes hold great promise for applications in various industries including food, medicine, environmental protection, agriculture, detergents, dyes, and others. Scientific studies on microbial-derived STPs have been widely reported, but there has been little systematic review of microbial-derived STPs and their application in high-salt conventional soybean fermentable foods. This review presents the STP-producing microbial species and their selection methods, and summarizes and analyzes the salt tolerance mechanisms of the microorganisms. It also outlines various techniques for the isolation and purification of STPs from microorganisms and discusses the salt tolerance mechanisms of STPs. Furthermore, this review demonstrates the contribution of modern biotechnology in the screening of novel microbial-derived STPs and their improvement in salt tolerance. It highlights the potential applications and commercial value of salt-tolerant microorganisms and STPs in high-salt traditional soy fermented foods. The review ends with concluding remarks on the challenges and future directions for microbial-derived STPs. This review provides valuable insights into the separation, purification, performance enhancement, and application of microbial-derived STPs in traditional fermented foods. Graphical Abstract

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“…Proteases, according to their optimum pH reactions, are classified as neutral protease, acidic protease and alkaline protease [7]. Neutral proteases are broadly applied in the food [8,], feed [9], pharmaceutical [10] and leather [11] industries due to their divergent benefits, including low pollution level, a mild catalysis process and high yield. Neutral protease is usually used for brewing beer [12] and de-bittering soy sauce in the food industry [13].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Cotton Seeds as Environmentally Liable Source for Neutral Protease

Shaikh¹,

Bhatti²

2022

Pak J Anal Environ Chem

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Proteases are considered one of the most imperative groups of enzymes and are used in bioremediation processes, leather, detergents, pharmaceutical and the food industry. The foremost aim of this study was to extract, purify, and characterize the protease enzyme from cotton seeds. Purification of the neutral protease was achieved with ammonium sulphate, which gave the best results at 60% concentration with a specific activity of 51 units/mg protein and 1.52 purification fold with a percentage yield of 10.5%. The protease was active and stable at a wide range of pH from 4.0–10.0 with an optimum pH of 7.0. The highest activity of the purified enzyme was found at 20 °C. The enzyme was thermally stable and retained 25% of its activity at 50o C. The activity of cottonseeds protease Fraction-IV was enhanced by 20% with ZnCl2 and 15% with CoCl2 as enzyme samples were heated for 10 minutes. The Casein and peptone assays were also performed to check its catalytic activity. Furthermore, the maximum hydrolysis rate (Vmax) and apparent Michaelis–Menten constant (Km) values of the purified protease were 19 μmol/min and 0.08 mol/L, respectively, while activation energy was found to be 12.47 KJ/mol.

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Expression of key hydrolases for soy sauce fermentation in Zygosaccharomyces rouxii

Cited by 15 publications

References 8 publications

Purification and characterization of neutral protease from Aspergillus oryzae Y1 isolated from naturally fermented broad beans

Purification and characterization of neutral protease from Aspergillus oryzae Y1 isolated from naturally fermented broad beans

Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review

Evaluation of Cotton Seeds as Environmentally Liable Source for Neutral Protease

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