Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

Ji, Dawei; Ma, Jingying; Xu, Min; Agyei, Dominic

doi:10.1111/1541-4337.12676

Cited by 44 publications

(57 citation statements)

References 196 publications

(307 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Temperatures above that are optimal for bacterial growth rapidly inactivate proteolytic enzymes. In some cases, irreversible loss of proteolytic enzyme activity is observed after prolonged storage at low temperatures [ 22 , 23 , 24 ]. Many proteolytic bacteria have psychrotrophic properties.…”

Section: Characteristics Of Lactic Acid Bacteriamentioning

confidence: 99%

“…The first domain occurring at the N-terminus of the enzyme molecule is a preprodome (PP) composed of a signal peptide containing 40 residues and a pro sequence containing 150 residues. The pro sequence section is removed by the autocatalysis process involving the PrtM protein located outside the cell membrane [ 23 , 67 ]. The PP domain is followed by a catalytic serine protease (PR) domain of 500 residues.…”

Section: Structure Of Extracellular Proteinasesmentioning

confidence: 99%

“…Domain B has been found in most extracellular proteinases, but it is not present in Lc. thermophilus [ 4 , 23 ].…”

Section: Structure Of Extracellular Proteinasesmentioning

confidence: 99%

“…Extracellular proteins still include a hydrophilic W domain composed of 100 amino acid residues. This domain contains a typical amino acid composition that is rich in Pro-Gly and Ser-Thr and is similar to the cell wall domain of gram-positive bacteria [ 23 ]. In PrtP, PrtS, and PrtR, the W domain has a cell wall anchoring domain (AN) behind it.…”

Section: Structure Of Extracellular Proteinasesmentioning

confidence: 99%

See 3 more Smart Citations

Characteristics of the Proteolytic Enzymes Produced by Lactic Acid Bacteria

et al. 2021

View full text Add to dashboard Cite

Over the past several decades, we have observed a very rapid development in the biotechnological use of lactic acid bacteria (LAB) in various branches of the food industry. All such areas of activity of these bacteria are very important and promise enormous economic and industrial successes. LAB are a numerous group of microorganisms that have the ability to ferment sugars into lactic acid and to produce proteolytic enzymes. LAB proteolytic enzymes play an important role in supplying cells with the nitrogen compounds necessary for their growth. Their nutritional requirements in this regard are very high. Lactic acid bacteria require many free amino acids to grow. The available amount of such compounds in the natural environment is usually small, hence the main function of these enzymes is the hydrolysis of proteins to components absorbed by bacterial cells. Enzymes are synthesized inside bacterial cells and are mostly secreted outside the cell. This type of proteinase remains linked to the cell wall structure by covalent bonds. Thanks to advances in enzymology, it is possible to obtain and design new enzymes and their preparations that can be widely used in various biotechnological processes. This article characterizes the proteolytic activity, describes LAB nitrogen metabolism and details the characteristics of the peptide transport system. Potential applications of proteolytic enzymes in many industries are also presented, including the food industry.

show abstract

Section: Characteristics Of Lactic Acid Bacteriamentioning

confidence: 99%

Section: Structure Of Extracellular Proteinasesmentioning

confidence: 99%

“…Domain B has been found in most extracellular proteinases, but it is not present in Lc. thermophilus [ 4 , 23 ].…”

Section: Structure Of Extracellular Proteinasesmentioning

confidence: 99%

Section: Structure Of Extracellular Proteinasesmentioning

confidence: 99%

See 2 more Smart Citations

Characteristics of the Proteolytic Enzymes Produced by Lactic Acid Bacteria

et al. 2021

View full text Add to dashboard Cite

show abstract

“…delbrueckii BD7. Additionally, Ji et al (2021) stated that the CEP properties of Lb. delbrueckii is a zinc-dependent monomer ∼70kDa, which degrades intact casein with a significant preference for βcasein.…”

Section: Identification Of Peptides Generated From Goat Milk Fermented By Lb Delbrueckii Ssp Delbrueckii Bd7 In the <3 Kda Fractionmentioning

confidence: 99%

Peptide profiling of goat milk fermented by Lactobacillus delbrueckii ssp. delbrueckii BD7: Identification of potential biological activity

et al. 2021

View full text Add to dashboard Cite

Abstract. Rubak YT, Nuraida L, Iswantini D, Prangdimurti E, Sanam MUE. 2021. Peptide profiling of goat milk fermented by Lactobacillus delbrueckii ssp. delbrueckii BD7: Identification of potential biological activity. Biodiversitas 22: 3136-3145. This study investigated the angiotensin-converting enzyme (ACE) inhibitory activity in fermented goat milk by Lactobacillus delbrueckii ssp. delbrueckii BD7, characterizing the peptide and its potential as a bioactive peptide. The starter culture (2%) was inoculated into pasteurized goat skim milk (11%), then incubated at 37 °C until it reached pH 4.6. Centrifugation at 6000 g x 10 minutes at 4 °C was applied. The supernatant obtained was then ultrafiltrated using a membrane cut-off with a molecular weight of 3 kDa, and the fraction obtained was analyzed to determine the inhibitory activity of ACE. Peptides were characterized using Nano LC / MS / MS, and identification as bioactive peptides was carried out based on a literature review. ACE inhibitory activity of fermented goat milk of Lb. delbrueckii ssp. delbrueckii BD7 was 55.98 ± 3.53%. A total of 157 peptides were released with molecular weights ranging from 770.78 - 2081.12 Da and having 7-19 amino acid residues. The main peptide was hydrolyzed from casein (72.6%), cleavage in the parent protein, specific for aliphatic and aromatic amino acids. Identification of bioactive peptides based on the similarity of amino acid residues at C-terminal obtained 28 ACE inhibitor peptides, 19 antioxidant peptides, and ten antimicrobial peptides. Some of these peptides have homologous sequences with previously reported peptides. Lb. delbrueckii ssp. delbrueckii BD7 has the potential as a starter culture to produce fermented milk, which is rich in biological activity.

show abstract