Federal Register / Vol. 62, No. 212 / Monday, November 3, 1997 / Rules and Regulations 59281

85–02–05, Amendment 39–4984, and by

adding a new AD to read as follows:

85–02–05 R1 The New Piper Aircraft, Inc.:

Amendment 39–10189; Docket No. 84–

CE–27–AD. Revises AD 85–02–05,

Amendment 39–4984.

Applicability: The following model and

serial number airplanes, certificated in any

category:

Models Serial numbers

PA–20, PA–20S, PA–

20–115, PA–20S–

115, PA–20–135,

and PA–20S–135.

20–1 through 20–

1121.

PA–22, PA–22–108,

PA–22–135, PA–

22S–135, PA–22–

150, PA–22S–150,

PA–22–160, and

PA–22S–160.

22–1 through 22–

9848.

PA–23 and PA–23–

160.

23–1 through 23–

2046.

PA–23–235, PA–23–

250, and PA–E23–

250.

27–1 through 27-

8154030.

PA–24, PA–24–250,

and PA–24–260.

24–1 through 24–

5034.

PA–24–400 ................ 26–1 through 26–148.

PA–25, PA–25–235,

and PA–25–260.

25–1 through 25-

8156024.

PA–30 ........................ 30–1 through 30–

2000.

PA–31P ..................... 31P–1 through 31P–

7730012.

PA–36–285, PA–36–

300, and PA–36–

375.

36–7360001 through

36–8302025.

PA–39 ........................ 39–1 through 39–162.

PA–44–180 ................ 44–7995001 through

44–8195026.

PA–44–180T ............. 44–8107001 through

44–8207020.

Note 1: This AD applies to each airplane

identified in the preceding applicability

provision, regardless of whether it has been

modified, altered, repaired, or reconfigured

in the area subject to the requirements of this

AD. For airplanes that have been modified,

altered, repaired, or reconfigured so that the

performance of the requirements of this AD

is affected, the owner/operator must request

approval for an alternative method of

compliance in accordance with paragraph (d)

of this AD. The request should include an

assessment of the effect of the modification,

alteration, or repair on the unsafe condition

addressed by this AD; and, if the unsafe

condition has not been eliminated, the

request should include specific proposed

actions to address it.

Compliance: Required within 100 hours

time-in-service after March 1, 1985 (the

effective date of AD 85–02–05, Amendment

39–4984) or prior to the next flight after the

effective date of this AD, whichever occurs

later, unless already accomplished.

To prevent airplane controllability

problems while involved in ground operation

because of improper brake operations,

accomplish the following:

(a) Install one of the following in a central

location on the pilot’s instrument panel in

full view of the pilot.

(1) A Piper part number 81090–02 placard;

or

(2) A Piper part number 683–107 placard.

Note 2: The above referenced placards both

contain the following language:

‘‘Warning No Braking Will Occur if

Aircraft Brakes Are Applied While

Parking Brake Handle is Pulled and

Held’’

(b) Special flight permits may be issued in

accordance with sections 21.197 and 21.199

of the Federal Aviation Regulations (14 CFR

21.197 and 21.199) to operate the airplane to

a location where the requirements of this AD

can be accomplished.

(c) Installing the placard required by

paragraph (a) of this AD may be performed

by the owner/operator holding at least a

private pilot certificate as authorized by

section 43.7 of the Federal Aviation

Regulations (14 CFR 43.7), and must be

entered into the aircraft records showing

compliance with this AD in accordance with

section 43.9 of the Federal Aviation

Regulations (14 CFR 43.9).

(d) An alternative method of compliance or

adjustment of the compliance time that

provides an equivalent level of safety may be

approved by the Manager, Atlanta Aircraft

Certification Office (ACO), One Crown

Center, 1895 Phoenix Boulevard, suite 450,

Atlanta, Georgia 30349.

(1) The request shall be forwarded through

an appropriate FAA Maintenance Inspector,

who may add comments and then send it to

the Manager, Atlanta ACO.

(2) Alternative methods of compliance

approved in accordance with AD 85–02–05

(revised by this action) are considered

approved as alternative methods of

compliance with this AD.

Note 3: Information concerning the

existence of approved alternative methods of

compliance with this AD, if any, may be

obtained from the Atlanta ACO.

(e) All persons affected by this directive

may examine information pertaining to this

document at the FAA, Central Region, Office

of the Regional Counsel, Room 1558, 601 E.

12th Street, Kansas City, Missouri 64106.

(f) This amendment (39–10189) becomes

effective on November 21, 1997.

Issued in Kansas City, Missouri, on

October 27, 1997.

Mary Ellen A. Schutt,

Acting Manager, Small Airplane Directorate,

Aircraft Certification Service.

[FR Doc. 97–28983 Filed 10–31–97; 8:45 am]

BILLING CODE 4910–13–P

DEPARTMENT OF HEALTH AND

HUMAN SERVICES

Food and Drug Administration

21 CFR Part 173

[Docket No. 93F–0461]

Secondary Direct Food Additives

Permitted in Food for Human

Consumption; Milk-Clotting Enzymes

AGENCY: Food and Drug Administration,

HHS.

ACTION: Final rule.

SUMMARY: The Food and Drug

Administration (FDA) is amending the

food additive regulations to provide for

the safe use of aspartic proteinase

enzyme preparation produced by pure

culture fermentation of Aspergillus

oryzae modified by recombinant

deoxyribonucleic (DNA) techniques to

contain the gene for aspartic proteinase

enzyme from Rhizomucor miehei for use

as a milk-clotting enzyme in the

production of cheese.

DATES: The regulation is effective

November 3, 1997; written objections

and requests for a hearing by December

3, 1997.

ADDRESSES: Submit written objections to

the Dockets Management Branch (HFA–

305), Food and Drug Administration,

12420 Parklawn Dr., rm. 1–23,

Rockville, MD 20857.

FOR FURTHER INFORMATION CONTACT:

Wendy J. Dixon, Center for Food Safety

and Applied Nutrition (HFS–206), Food

and Drug Administration, 200 C St. SW.,

Washington, DC 20204, 202–418–3090.

SUPPLEMENTARY INFORMATION:

In a notice published in the Federal

Register of January 21, 1994 (59 FR

3365), FDA announced that a food

additive petition (FAP 4A4406) had

been filed by Novo Nordisk

Bioindustrials, Inc., proposing that the

food additive regulations be amended to

provide for the safe use of aspartic

proteinase enzyme preparation

produced by pure culture fermentation

of A. oryzae modified by recombinant

DNA techniques to contain the gene for

aspartic proteinase enzyme from R.

miehei for use in the production of

cheese. Although Novo Nordisk

Bioindustrials, Inc., submitted FAP

4A4406, while the petition was under

review, Gist-Brocades International B.

V. purchased the dairy enzyme business

from Novo Nordisk, at which time, the

responsibility for the petition

transferred to Gist-Brocades

International B. V.
59282 Federal Register / Vol. 62, No. 212 / Monday, November 3, 1997 / Rules and Regulations

1SDS–PAGE is a technique that enables one to

compare the relative molecular weight of proteins

based on their rate of migration through the gel. The

SDS-PAGE relative mobility of a protein is directly

related to its molecular weight.

I. Evaluation of Safety of the Petitioned

Use of the Additive

A. Aspergillus Oryzae

The host organism for production of

aspartic proteinase is the fungus A.

oryzae. A. oryzae has had a long history

of use, greater than 2,000 years, in the

production of enzymes, e.g., koji and αamylase, used in the fermentation and

processing of food products, such as

soy-sauce, miso, sake, baked goods, and

brewery products (Refs. 1 and 2). The

nonpathogenicity and nontoxigenicity

of this microbe to humans and its

inability to produce antibiotics is welldocumented in the literature (Refs. 1, 3,

and 4). This conclusion regarding the

nonpathogenicity and nontoxigenicity

of this microbe is consistent with a

recent evaluation of the Joint Expert

Committee on Food Additives (JECFA)

of the Food and Agriculture

Organization (FAO) and the World

Health Organization (WHO) (Ref. 5).

JECFA evaluated the current uses of A.

oryzae and enzyme preparations

therefrom and concluded that the

amylases and proteases from A. oryzae

that were included in JECFA’s review

should be regarded as foods and thus,

are safe for use in food processing.

The petitioner submitted a study to

investigate the pathogenic potential of

five strains of A. oryzae, including the

parental strain and four recombinant

strains; one of the strains tested is the

subject of this petition. FDA evaluated

this study and concluded that the

recombinant strains of A. oryzae, as well

as the unmodified parental strain,

demonstrated no pathogenicity for mice

when spores were inoculated in large

numbers. Previously, A. oryzae has been

the subject of evaluations performed by

FDA, and based on those evaluations

FDA concluded that the spores of two

strains of A. oryzae are nonpathogenic

to mice (Ref. 6). Therefore, FDA

concludes that the recombinant strain of

A. oryzae that is the subject of this

petition is nonpathogenic and

nontoxigenic (Ref. 3).

B. Rhizomucor Miehei

R. miehei, originally named Mucor

miehei (Ref. 7), is the microorganism

used as the source of the genetic

material for the aspartic proteinase

enzyme that is the subject of FAP

4A4406. Enzyme preparations derived

from R. miehei (aspartic proteinase, or

esterase-lipase activity produced by

pure culture fermentation of R. miehei

(as M. miehei)) are food additives that

are approved for use in cheese

production under §§ 173.150(a)(4) and

173.140 (21 CFR 173.150(a)(4) and

173.140), respectively.

C. Aspartic Proteinase Preparation

As discussed above, aspartic

proteinase preparation produced by

pure culture fermentation of R. miehei

for use as a milk-clotting agent in the

production of cheese is an approved

food additive under § 173.150(a)(4). The

petitioner has submitted the following

evidence to demonstrate that it has

cloned full length copies of the aspartic

proteinase gene from R. miehei into A.

oryzae: (1) DNA sequencing

information, whereby the cloned

putative aspartic proteinase gene was

shown to have the same nucleotide

sequence that encodes the amino acid

sequence of the R. miehei aspartic

proteinase; and (2) nucleic acid

hybridization studies whereby the

cloned DNA fragments were shown to

hybridize (i.e., specifically bind) with

complementary DNA from the aspartic

proteinase gene.

To further confirm the identity of the

aspartic proteinase cloned into A.

oryzae, the petitioner provided

information on the sodium dodecyl

polyacrylamide gel electrophoresis

(SDS–PAGE)1 relative mobility of

recombinant aspartic proteinase and

aspartic proteinase from R. miehei, with

and without treatment by endoglucosidase H (an enzyme that removes

most glycosyl moieties from proteins).

The results from this study establish

that untreated aspartic proteinase from

recombinant A. oryzae has a lower

relative mobility than untreated aspartic

proteinase from R. miehei. However,

after pretreatment with endoglucosidase H, the aspartic proteinase

preparations from both recombinant A.

oryzae and R. miehei have an identical

SDS–PAGE relative mobility. This is

higher than the mobilities of either of

the untreated forms of aspartic

proteinase. These results show that

aspartic proteinase from A. oryzae or R.

miehei is glycosylated but when the R.

miehei gene for aspartic proteinase is

expressed in A. oryzae, the aspartic

proteinase enzyme is more extensively

glycosylated (Ref. 8).

FDA finds that glycosylation of the

aspartic proteinase enzyme does not

raise any safety concerns. Glycosylation

is characteristic of many proteins

produced in the cells of eukaryotic

organisms, which include higher plants

and animals, and fungi, such as A.

oryzae and R. miehei (Ref. 9). However,

the type and amount of glycosyl

moieties attached to glycoproteins

varies, even among closely related

organisms (Ref. 10). Therefore, proteins

with identical amino acid sequences

may have different amounts and types

of glycosylation when produced in

different eukaryotic organisms, such as

A. oryzae and R. miehei. Because A.

oryzae is a common, nonpathogenic,

nontoxigenic organism that has a safe

history of use in the production of food

processing enzymes (Refs. 1 and 3), the

agency finds that the more extensively

glycosylated aspartic proteinase enzyme

from recombinant A. oryzae is as safe as

the less extensively glycosylated

aspartic proteinase enzyme from R.

miehei.

The petitioner submitted several

toxicological studies that address the

safety of the petitioned aspartic

proteinase preparation. These include:

(1) Short term and subchronic toxicity

studies in both rats and dogs; (2) a

teratogenicity study in rats; and (3)

genotoxicity studies, including tests for

mutagenic activity in Salmonella

typhimurium and mammalian cells, as

well as tests for chromosome-damaging

activity in human lymphocytes. FDA

has reviewed these studies and

concludes that the petitioned aspartic

proteinase preparation does not raise

any toxicity concerns at the expected

level of consumption nor does it have

any mutagenic potential (Refs. 6, 11,

and 12).

D. Source of Impurities

Enzyme preparations used in food are

usually not chemically pure, but contain

cellular and processing material. The

nature and amounts of these impurities

in the finished enzyme preparation

depend on the organism from which the

enzyme preparation is produced (the

production organism), the fermentation

materials and methods used to grow the

production organism, and the materials

and methods used to generate the

finished enzyme preparation. Thus, the

question is whether the production

organism or the manufacturing methods

used to grow the production organism

or to generate the finished enzyme

preparation from recombinant A.

oryzae, will introduce impurities that

raise concerns about the safety of the

enzyme preparation. In addition,

§ 173.150(c) states that the milk-clotting

enzyme preparation shall be produced

by a process that completely removes

the generating organism from the milkclotting enzyme product. The agency

concludes that the petition contains

information demonstrating that the

manufacturing process includes

procedures to ensure that the

production organism is completely

removed from the enzyme preparation
Federal Register / Vol. 62, No. 212 / Monday, November 3, 1997 / Rules and Regulations 59283

during the manufacturing (Refs. 3 and

13).

One issue raised by the use of

recombinant DNA techniques is the

potential transfer of DNA encoding for

extraneous proteins along with the gene

of interest (i.e., aspartic proteinase),

thereby contaminating the enzyme

preparation. As a matter of current good

manufacturing practice, manufacturers

using recombinant DNA technology

should ensure that they have not

inadvertently cloned extraneous

protein-encoding DNA along with the

aspartic proteinase gene that may lead

to contamination of the aspartic

proteinase enzyme preparation. Such

assurance can come from reviewing the

details of the cloning steps, which

include the origin and sequence of the

DNA fragments used in the cloning, and

full characterization of the final genetic

constructs via techniques such as DNA

sequencing.

The petition contains information

demonstrating that the petitioner

evaluated the cloning process to ensure

that the final cloning product, i. e., the

DNA with the aspartic proteinase gene

and other components to ensure

accurate expression of the gene, used in

the development of the recombinant A.

oryzae was accurately constructed. As

mentioned above, the petitioner

submitted evidence to demonstrate that

it cloned full length copies of the

aspartic proteinase gene from R. miehei

into A. oryzae. In addition to the

aspartic proteinase gene, the

recombinant A. oryzae strain contains a

marker gene conferring resistance to

ampicillin (ampr), a clinically useful

antibiotic, as well as a marker gene

encoding the enzyme acetamidase

(amdS), which permits the transformed

strain to utilize acetamide as a nitrogen

or carbon source. The petitioner states

that the only transgenes expressed in

the production organism, A. oryzae, are

the aspartic proteinase transgene and

the amdS transgene. Aspartic proteinase

is secreted into the culture medium

from which the enzyme preparation is

produced while the enzyme

acetamidase is not. Therefore, the

agency concludes that the acetamidase

is effectively removed when the

production cells are discarded during

processing (Ref. 13).

The expression of the ampr gene is

controlled by a promoter, a region of

DNA that is a major component in the

regulation of a gene. In general, bacterial

promoters do not function in higher

organisms, including the fungus A.

oryzae. Because expression of the ampr

gene is controlled by a bacterial

promoter, this gene is not expected to be

expressed in the production organism,

A. oryzae. The agency has considered

the potential consequences if expression

of the ampr transgene were to occur in

the production organism. The petitioner

noted that the enzyme preparation is

produced from the fermentation

supernatant and that in the process,

intact cells are removed. Therefore, even

if expression of the ampr gene takes

place, the gene product would be

sequestered within the intact cells and

therefore, would not be present in the

fermentation supernatant, which is the

source of the aspartic proteinase enzyme

preparation. Accordingly, the agency

concludes that any ampr gene product

would effectively be removed from the

enzyme preparation (Ref. 13).

Finally, FDA notes that § 173.150(b)

stipulates that the microbial milkclotting enzyme listed in the food

additive regulations should be produced

using a production strain that is

nonpathogenic and nontoxic in man or

other animals. For example, if the DNA

inserted by recombinant methodology

were to encode a toxic substance that

would render the enzyme preparation

unsafe, the resulting aspartic proteinase

preparation would not conform with the

prescribed conditions under § 173.150,

and therefore, food processed with the

improperly manufactured enzyme

preparation would be deemed

adulterated.

FDA concludes that, when the

aspartic proteinase preparation is

manufactured in conformity with

§ 173.150, there is no basis for concern

regarding the possibility that the

aspartic proteinase preparation will be

contaminated by the products of

extraneous protein-encoding DNA (e.g.,

products of amdS and ampr genes)

inserted along with the aspartic

proteinase gene in A. oryzae (Ref. 13).

Furthermore, FDA concludes, having

considered the evidence concerning the

production organism and the processing

steps to derive the aspartic proteinase

preparation, that A. oryzae containing

aspartic proteinase gene from R. miehei

is safe for use as a source of food-grade

aspartic proteinase preparations, and

that impurities resulting from the use of

A. oryzae containing aspartic proteinase

gene from R. miehei in the production

of aspartic proteinase preparation will

not affect the safety of the aspartic

proteinase preparation.

II. Conclusion

The agency finds that the principal

active ingredient, i.e., aspartic

proteinase, in the aspartic proteinase

enzyme preparation, is the same as that

in the milk-clotting enzyme preparation

from R. miehei, and that when the

preparation is manufactured in

accordance with the conditions of use

listed in § 173.150, the source organism

and manufacturing process will not

introduce impurities that may render

the use of the enzyme preparation

unsafe.

The agency has evaluated the data in

the petition and other relevant material.

Based on this information, the agency

concludes that the proposed use of

aspartic proteinase enzyme preparation

from A. oryzae containing the aspartic

proteinase gene from R. miehei is safe

and that the additive will achieve its

intended technical effect. Therefore, the

regulation in § 173.150 should be

amended.

III. Inspection of Documents

In accordance with § 171.1(h) (21 CFR

171.1(h)), the petition and the

documents that FDA considered and

relied upon in reaching its decision to

approve the petition are available for

inspection at the Center for Food Safety

and Applied Nutrition by appointment

with the information contact person

listed above. As provided in § 171.1(h),

the agency will delete from the

documents any materials that are not

available for public disclosure before

making the documents available for

inspection.

IV. Environmental Impact

The agency has carefully considered

the potential environmental effects of

this action. FDA has concluded that the

action will not have a significant impact

on the human environment, and that an

environmental impact statement is not

required. The agency’s finding of no

significant impact and the evidence

supporting that finding, contained in an

environmental assessment, may be seen

in the Dockets Management Branch

(address above) between 9 a.m. and 4

p.m., Monday through Friday.

V. Objections

Any person who will be adversely

affected by this regulation may at any

time on or before December 3, 1997, file

with the Dockets Management Branch

(address above) written objections

thereto. Each objection shall be

separately numbered, and each

numbered objection shall specify with

particularity the provisions of the

regulation to which objection is made

and the grounds for the objection. Each

numbered objection on which a hearing

is requested shall specifically so state.

Failure to request a hearing for any

particular objection shall constitute a

waiver of the right to a hearing on that

objection. Each numbered objection for

which a hearing is requested shall

include a detailed description and
59284 Federal Register / Vol. 62, No. 212 / Monday, November 3, 1997 / Rules and Regulations

analysis of the specific factual

information intended to be presented in

support of the objection in the event

that a hearing is held. Failure to include

such a description and analysis for any

particular objection shall constitute a

waiver of the right to a hearing on the

objection. Three copies of all documents

shall be submitted and shall be

identified with the docket number

found in brackets in the heading of this

document. Any objections received in

response to the regulation may be seen

in the Dockets Management Branch

between 9 a.m. and 4 p.m., Monday

through Friday.

VI. References

The following references have been

placed on display in the Dockets

Management Branch (address above)

and may be seen by interested persons

between 9 a.m. and 4 p.m., Monday

through Friday.

1. Barbesgaard, P., H. P. Heldt-Hansen, and

B. Diderichsen, ‘‘On the Safety of Aspergillus

oryzae: A Review,’’ Applied Microbiology

and Biotechnology, 36:569–572, 1992.

2. ‘‘Biotechnologies and Food: Assuring the

Safety of Foods Produced by Genetic

Modification,’’ Regulatory Toxicology and

Pharmacology, 12 (3):S114–S128, 1990.

3. Memorandum from J. Madden, FDA, to

D. Keefe, FDA, April 11, 1994.

4. Gray, W. D., The Use of Fungi as Food

and in Food Processing, pp. 42–100, CRC

Press, Cleveland, OH, 1970.

5. Joint FAO/WHO Expert Committee on

Food Additives. ‘‘Toxicological Evaluation of

Certain Food Additives,’’ 31st Meeting,

Geneva, February 16–25, 1987.

6. Memorandum from H. C. A. Chang,

FDA, to D. Keefe, FDA, March 14, 1994.

7. Shipper, M. A. A., ‘‘On the Genera

Rhizomucor and Parasitella,’’ Studies in

Mycology, 17:53–65, 1978.

8. Cristensen, T. et al., ‘‘High Level

Expression of Recombinant Genes in

Aspergillus oryzae,’’ Bio/Technology,

6:1419–1422, 1988.

9. Herrman, J. L. et al., ‘‘Bacterial

Glycoproteins: A Link Between Glycosylation

and Proteolytic Cleavage of a 19 kDa Antigen

from Mycobacterium tuberculosis,’’ EMBO

Journal, 15:3547–3554, 1996.

10. Grinna, L. S., and J. F. Tschopp, ‘‘Size

Distribution and General Structural Features

of N-linked Oligosaccharides from the

Methylotrophic Yeast, Pichia pastoris,’’

Yeast, 5 (2):107–115, 1989.

11. Memorandum from S. E. Carberry,

FDA, to D. Keefe, FDA, January 5, 1995.

12. Memorandum from H. C. A. Chang,

FDA, to D. Keefe, FDA, February 6, 1995.

13. Memorandum from T. A. Cebula, FDA,

to D. Keefe, FDA, April 4, 1995.

List of Subjects in 21 CFR Part 173

Food additives.

Therefore, under the Federal Food,

Drug, and Cosmetic Act and under

authority delegated to the Commissioner

of Food and Drugs and redelegated to

the Director, Center for Food Safety and

Applied Nutrition, 21 CFR part 173 is

amended as follows:

PART 173—SECONDARY DIRECT

FOOD ADDITIVES PERMITTED IN

FOOD FOR HUMAN CONSUMPTION

1. The authority citation for 21 CFR

part 173 continues to read as follows:

Authority: 21 U.S.C. 321, 342, 348.

2. Section 173.150 is amended by

adding paragraph (a)(5) to read as

follows:

§ 173.150 Milk-clotting enzymes, microbial.

* * * * *

(a) * * *

(5) Aspergillus oryzae modified by

recombinant deoxyribonucleic (DNA)

techniques to contain the gene coding

for aspartic proteinase from Rhizomucor

miehei var. Cooney et Emerson as

defined in paragraph (a)(4) of this

section, and classified as follows: Class,

Blastodeuteromycetes (Hyphomycetes);

order, Phialidales (Moniliales); genus,

Aspergillus; species oryzae.

Dated: October 20, 1997.

L. Robert Lake,

Director, Office of Policy, Planning and

Strategic Initiatives, Center for Food Safety

and Applied Nutrition.

[FR Doc. 97–29048 Filed 10–31–97; 8:45 am]

BILLING CODE 4160–01–F

ENVIRONMENTAL PROTECTION

AGENCY

40 CFR Part 52

[CA 083–0053a; FRL–5911–4]

Approval and Promulgation of

Implementation Plans; California State

Implementation Plan Revision, San

Diego County Air Pollution Control

District, Ventura County Air Pollution

Control District

AGENCY: Environmental Protection

Agency (EPA).

ACTION: Direct final rule.

SUMMARY: EPA is taking direct final

action on revisions to the California

State Implementation Plan (SIP). These

revisions concern rules from the San

Diego County Air Pollution Control

District (SDCAPCD) and the Ventura

County Air Pollution Control District

(VCAPCD). This approval action will

incorporate these rules into the federally

approved SIP. The intended effect of

approving these rules is to regulate

emissions of volatile organic

compounds (VOCs) in accordance with

the requirements of the Clean Air Act,

as amended in 1990 (CAA or the Act).

The revised rules control VOC

emissions from metal container, metal

closure, and metal coil coating

operations and marine vessel coating

operations. Thus, EPA is finalizing the

approval of these revisions into the

California SIP under provisions of the

CAA regarding EPA action on SIP

submittals, SIPs for national primary

and secondary ambient air quality

standards and plan requirements for

nonattainment areas.

DATES: This action is effective on

January 2, 1998 unless adverse or

critical comments are received by

December 3, 1997. If the effective date

is delayed, timely notice will be

published in the Federal Register.

ADDRESSES: Comments must be

submitted to Andrew Steckel at the

Region IX office listed below. Copies of

the rule revisions and EPA’s evaluation

report for each rule are available for

public inspection at EPA’s Region IX

office during normal business hours.

Copies of the submitted rule revisions

are available for inspection at the

following locations:

Rulemaking Office (AIR–4), Air

Division, U.S. Environmental

Protection Agency, Region IX, 75

Hawthorne Street, San Francisco, CA

94105

Environmental Protection Agency, Air

Docket (6102), 401 ‘‘M’’ Street, S.W.,

Washington, D.C. 20460

California Air Resources Board,

Stationary Source Division, Rule

Evaluation Section, 2020 ‘‘L’’ Street,

Sacramento, CA 92123–1095

San Diego County Air Pollution Control

District, 9150 Chesapeake Drive, San

Diego, CA 92123–1096

Ventura County Air Pollution Control

District, 702 County Square Drive,

Ventura, California 93003.

FOR FURTHER INFORMATION CONTACT:

Jerald S. Wamsley, Rulemaking Office,

AIR–4, Air Division, U.S.

Environmental Protection Agency,

Region IX, 75 Hawthorne Street, San

Francisco, CA 94105, Telephone: (415)

744–1226

SUPPLEMENTARY INFORMATION:

I. Applicability

The rules being approved into the

California SIP include SDCAPCD’s Rule

67.4, Metal Container, Metal Closure,

and Metal Coil Coating Operations, and

VCAPCD’s Rule 74.24, Marine Vessel

Coating Operations. These rules were

submitted by the California Air

Resources Board (CARB) to EPA on

October 18, 1996 and May 24, 1994,

respectively.